BMRB Entry 18620
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18620
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Title: NMR Chemical Shift Assignments of N terminal RRM domain of La protein PubMed: 23239108
Deposition date: 2012-07-27 Original release date: 2013-02-14
Authors: Bouras, Georgios; Argyriou, Aikaterini; Apostolidi, Maria; Chasapis, Christos; Stathopoulos, Constantinos; Bentrop, Detlef; Spyroulias, Georgios
Citation: Apostolidi, Maria; Vourtsis, Dionysios; Chasapis, Christos; Stathopoulos, Constantinos; Bentrop, Detlef; Spyroulias, Georgios. "H, 15N, 13C assignment and secondary structure determination of two domains of La protein from D. discoideum." Biomol. NMR Assignments 8, 47-51 (2014).
Assembly members:
RRM, polymer, 99 residues, 11412.86 Da.
Natural source: Common Name: Dictyostelium discoideum Taxonomy ID: 44689 Superkingdom: Eukaryota Kingdom: not available Genus/species: Dictyostelium discoideum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
RRM: GKTLYSKGWPEDTTIEKVQE
FFNANGGYKVVSVRLRKKSD
KSFKGSFLADFETEEIVNKI
ITEAPKLGEKELIYQTFKQF
SDEKKDEKEKFFASTNGDK
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 430 |
15N chemical shifts | 102 |
1H chemical shifts | 536 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | RRM domain | 1 |
Entities:
Entity 1, RRM domain 99 residues - 11412.86 Da.
1 | GLY | LYS | THR | LEU | TYR | SER | LYS | GLY | TRP | PRO | ||||
2 | GLU | ASP | THR | THR | ILE | GLU | LYS | VAL | GLN | GLU | ||||
3 | PHE | PHE | ASN | ALA | ASN | GLY | GLY | TYR | LYS | VAL | ||||
4 | VAL | SER | VAL | ARG | LEU | ARG | LYS | LYS | SER | ASP | ||||
5 | LYS | SER | PHE | LYS | GLY | SER | PHE | LEU | ALA | ASP | ||||
6 | PHE | GLU | THR | GLU | GLU | ILE | VAL | ASN | LYS | ILE | ||||
7 | ILE | THR | GLU | ALA | PRO | LYS | LEU | GLY | GLU | LYS | ||||
8 | GLU | LEU | ILE | TYR | GLN | THR | PHE | LYS | GLN | PHE | ||||
9 | SER | ASP | GLU | LYS | LYS | ASP | GLU | LYS | GLU | LYS | ||||
10 | PHE | PHE | ALA | SER | THR | ASN | GLY | ASP | LYS |
Samples:
sample_1: RRM, [U-98% 15N], 0.35 mM; buffer salts 50 mM
sample_2: RRM, [U-98% 13C; U-98% 15N], 0.35 mM; buffer salts 50 mM
sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 298 K
sample_conditions_2: ionic strength: 50 mM; pH: 7; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_2 |
3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_2 |
3D HNCO | sample_2 | isotropic | sample_conditions_2 |
3D HNCA | sample_2 | isotropic | sample_conditions_2 |
3D HNCACB | sample_2 | isotropic | sample_conditions_2 |
3D HN(CO)CA | sample_2 | isotropic | sample_conditions_2 |
3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_2 |
Software:
CARA v1.8.4, Keller and Wuthrich - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts