BMRB Entry 28085
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28085
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Title: 1H, 13C, and 15N backbone assignments of the C-terminal region of the human retinoic acid induced protein 2 PubMed: 32557393
Deposition date: 2020-02-18 Original release date: 2021-02-18
Authors: Lang, Andras; Goradia, Nishit; Wilmanns, Matthias; Ohlenschlaeger, Oliver
Citation: Lang, Andras; Goradia, Nishit; Wikman, Harriet; Werner, Stefan; Wilmanns, Matthias; Ohlenschlaeger, Oliver. "1H, 13C, and 15N backbone assignments of the C-terminal region of the human retinoic acid induced protein 2" Biomol. NMR Assignments 14, 271-275 (2020).
Assembly members:
RAI2, polymer, 153 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pETGB1a
Entity Sequences (FASTA):
RAI2: GAMDSRHTVIKMGSENEALD
LSMKSVPWLKAGEVSPPIFQ
EDAALDLSVAAHRKSEPPPE
TLYDSGASVDSSGHTVMEKL
PSGMEISFAPATSHEAPAMM
DSHISSSDAATEMLSQPNHP
SGEVKAENNIEMVGESQAAK
VIVSVEDAVPTIF
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 443 |
| 15N chemical shifts | 139 |
| 1H chemical shifts | 289 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RAI2 | 1 |
Entities:
Entity 1, RAI2 153 residues - Formula weight is not available
Residues 1-4 represent a non-native cloning artifact
| 1 | GLY | ALA | MET | ASP | SER | ARG | HIS | THR | VAL | ILE | ||||
| 2 | LYS | MET | GLY | SER | GLU | ASN | GLU | ALA | LEU | ASP | ||||
| 3 | LEU | SER | MET | LYS | SER | VAL | PRO | TRP | LEU | LYS | ||||
| 4 | ALA | GLY | GLU | VAL | SER | PRO | PRO | ILE | PHE | GLN | ||||
| 5 | GLU | ASP | ALA | ALA | LEU | ASP | LEU | SER | VAL | ALA | ||||
| 6 | ALA | HIS | ARG | LYS | SER | GLU | PRO | PRO | PRO | GLU | ||||
| 7 | THR | LEU | TYR | ASP | SER | GLY | ALA | SER | VAL | ASP | ||||
| 8 | SER | SER | GLY | HIS | THR | VAL | MET | GLU | LYS | LEU | ||||
| 9 | PRO | SER | GLY | MET | GLU | ILE | SER | PHE | ALA | PRO | ||||
| 10 | ALA | THR | SER | HIS | GLU | ALA | PRO | ALA | MET | MET | ||||
| 11 | ASP | SER | HIS | ILE | SER | SER | SER | ASP | ALA | ALA | ||||
| 12 | THR | GLU | MET | LEU | SER | GLN | PRO | ASN | HIS | PRO | ||||
| 13 | SER | GLY | GLU | VAL | LYS | ALA | GLU | ASN | ASN | ILE | ||||
| 14 | GLU | MET | VAL | GLY | GLU | SER | GLN | ALA | ALA | LYS | ||||
| 15 | VAL | ILE | VAL | SER | VAL | GLU | ASP | ALA | VAL | PRO | ||||
| 16 | THR | ILE | PHE |
Samples:
sample_1: RAI2, [U-99% 13C; U-99% 15N], 1 mM; TCEP 1.5 uM; sodium phosphate 20 mM; sodium chloride 50 mM
sample_conditions_1: ionic strength: 70 mM; pH: 6.8; pressure: 1 atm; temperature: 297 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 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | 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)N(COCA)NNH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v4.0.6, Bruker Biospin - collection, processing
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts