BMRB Entry 18621
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18621
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Title: NMR Chemical Shift Assignments of N terminal La motif 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:
La_motif, polymer, 91 residues, 10534.9 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):
La_motif: MSEETSTQILKQVEYYFSDS
NFPRDKFLRSEAAKNVDNYI
SIDVIASFNRMKTISTDLQL
ITEALKKSTRLQVSEDGKMV
RRLDPLPENID
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 383 |
15N chemical shifts | 88 |
1H chemical shifts | 514 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | La-type RNA-binding domain | 1 |
Entities:
Entity 1, La-type RNA-binding domain 91 residues - 10534.9 Da.
1 | MET | SER | GLU | GLU | THR | SER | THR | GLN | ILE | LEU | ||||
2 | LYS | GLN | VAL | GLU | TYR | TYR | PHE | SER | ASP | SER | ||||
3 | ASN | PHE | PRO | ARG | ASP | LYS | PHE | LEU | ARG | SER | ||||
4 | GLU | ALA | ALA | LYS | ASN | VAL | ASP | ASN | TYR | ILE | ||||
5 | SER | ILE | ASP | VAL | ILE | ALA | SER | PHE | ASN | ARG | ||||
6 | MET | LYS | THR | ILE | SER | THR | ASP | LEU | GLN | LEU | ||||
7 | ILE | THR | GLU | ALA | LEU | LYS | LYS | SER | THR | ARG | ||||
8 | LEU | GLN | VAL | SER | GLU | ASP | GLY | LYS | MET | VAL | ||||
9 | ARG | ARG | LEU | ASP | PRO | LEU | PRO | GLU | ASN | ILE | ||||
10 | ASP |
Samples:
sample_1: La-type RNA-binding domain, [U-98% 15N], 0.37 mM; buffer salts 50 mM
sample_2: La-type RNA-binding domain, [U-98% 13C; U-98% 15N], 0.37 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