BMRB Entry 19967
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19967
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Title: Solution NMR assignment of C-terminal RRM domain of La protein from D. discoideum. PubMed: 25281001
Deposition date: 2014-05-12 Original release date: 2018-02-27
Authors: Bouras, Georgios; Argyriou, Aikaterini; Makrynitsa, Garyfallia; Apostolidi, Maria; Chasapis, Christos; Stathopoulos, Constantinos; Bentrop, Detlef; Spyroulias, Georgios
Citation: Argyriou, Aikaterini; Chasapis, Christos; Apostolidi, Maria; Konstantinidou, Parthena; Stathopoulos, Constantinos; Bentrop, Detlef; Spyroulias, Georgios. "Backbone and side chain NMR assignment, along with the secondary structure prediction of RRM2 domain of La protein from a lower eukaryote exhibiting identical structural organization with its human homolog" Biomol NMR Assign. 9, 219-222 (2015).
Assembly members:
CRRM, polymer, 105 residues, 12027.6 Da.
Natural source: Common Name: cellular slime mold Taxonomy ID: 44689 Superkingdom: Eukaryota Kingdom: not available Genus/species: Dictyostelium discoideum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET
Entity Sequences (FASTA):
CRRM: KDVKKEVEEEEVMIPGVILC
FKGVGKGLHRGDIKEIFSQY
GEVQFVGYNSDEENGSVRYK
TAESCKRAIESLTETKKEIG
GQIPTYNLLEGEEEKKEWEK
IIERK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 460 |
| 15N chemical shifts | 108 |
| 1H chemical shifts | 743 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CRRM domain | 1 |
Entities:
Entity 1, CRRM domain 105 residues - 12027.6 Da.
| 1 | LYS | ASP | VAL | LYS | LYS | GLU | VAL | GLU | GLU | GLU | ||||
| 2 | GLU | VAL | MET | ILE | PRO | GLY | VAL | ILE | LEU | CYS | ||||
| 3 | PHE | LYS | GLY | VAL | GLY | LYS | GLY | LEU | HIS | ARG | ||||
| 4 | GLY | ASP | ILE | LYS | GLU | ILE | PHE | SER | GLN | TYR | ||||
| 5 | GLY | GLU | VAL | GLN | PHE | VAL | GLY | TYR | ASN | SER | ||||
| 6 | ASP | GLU | GLU | ASN | GLY | SER | VAL | ARG | TYR | LYS | ||||
| 7 | THR | ALA | GLU | SER | CYS | LYS | ARG | ALA | ILE | GLU | ||||
| 8 | SER | LEU | THR | GLU | THR | LYS | LYS | GLU | ILE | GLY | ||||
| 9 | GLY | GLN | ILE | PRO | THR | TYR | ASN | LEU | LEU | GLU | ||||
| 10 | GLY | GLU | GLU | GLU | LYS | LYS | GLU | TRP | GLU | LYS | ||||
| 11 | ILE | ILE | GLU | ARG | LYS |
Samples:
sample_1: CRRM, [U-99% 15N], 0.8 mM; H2O 90%; D2O 10%
sample_2: CRRM, [U-99% 13C; U-99% 15N], 0.8 mM; H2O 90%; D2O 10%
sample_3: CRRM 0.8 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_3 | isotropic | sample_conditions_1 |
Software:
CARA v1.8.4, Keller and Wuthrich - chemical shift assignment
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