BMRB Entry 52143
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52143
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Title: 1H, 15N and 13C chemical shift assignments for the D1 domain of the human DEAD-box RNA helicase DDX3X
Deposition date: 2023-09-19 Original release date: 2024-03-18
Authors: Toyama, Yuki; Shimada, Ichio
Citation: Toyama, Yuki; Shimada, Ichio. "NMR characterization of RNA binding property of the DEAD-box RNA helicase DDX3X and its implications for helicase activity" .
Assembly members:
entity_1, polymer, 279 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-SUMO
Entity Sequences (FASTA):
entity_1: GGDEDDWSKPLPPSERLEQE
LFSGGNTGINFEKYDDIPVE
ATGNNCPPHIESFSDVEMGE
IIMGNIELTRYTRPTPVQKH
AIPIIKEKRDLMACAQTGSG
KTAAFLLPILSQIYSDGPGE
ALRAMKENGRYGRRKQYPIS
LVLAPTRELAVQIYEEARKF
SYRSRVRPCVVYGGADIGQQ
IRDLERGCHLLVATPGRLVD
MMERGKIGLDFCKYLVLDEA
DRMLDMGFEPQIRRIVEQDT
MPPKGVRHTMMFSATFPKEI
QMLARDFLDEYIFLAVGRV
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 710 |
15N chemical shifts | 223 |
1H chemical shifts | 283 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | D1 domain | 1 |
Entities:
Entity 1, D1 domain 279 residues - Formula weight is not available
The first two Gly residues were introduced to facilitate the cleavage of N-terminal His-SUMO tag.
1 | GLY | GLY | ASP | GLU | ASP | ASP | TRP | SER | LYS | PRO | ||||
2 | LEU | PRO | PRO | SER | GLU | ARG | LEU | GLU | GLN | GLU | ||||
3 | LEU | PHE | SER | GLY | GLY | ASN | THR | GLY | ILE | ASN | ||||
4 | PHE | GLU | LYS | TYR | ASP | ASP | ILE | PRO | VAL | GLU | ||||
5 | ALA | THR | GLY | ASN | ASN | CYS | PRO | PRO | HIS | ILE | ||||
6 | GLU | SER | PHE | SER | ASP | VAL | GLU | MET | GLY | GLU | ||||
7 | ILE | ILE | MET | GLY | ASN | ILE | GLU | LEU | THR | ARG | ||||
8 | TYR | THR | ARG | PRO | THR | PRO | VAL | GLN | LYS | HIS | ||||
9 | ALA | ILE | PRO | ILE | ILE | LYS | GLU | LYS | ARG | ASP | ||||
10 | LEU | MET | ALA | CYS | ALA | GLN | THR | GLY | SER | GLY | ||||
11 | LYS | THR | ALA | ALA | PHE | LEU | LEU | PRO | ILE | LEU | ||||
12 | SER | GLN | ILE | TYR | SER | ASP | GLY | PRO | GLY | GLU | ||||
13 | ALA | LEU | ARG | ALA | MET | LYS | GLU | ASN | GLY | ARG | ||||
14 | TYR | GLY | ARG | ARG | LYS | GLN | TYR | PRO | ILE | SER | ||||
15 | LEU | VAL | LEU | ALA | PRO | THR | ARG | GLU | LEU | ALA | ||||
16 | VAL | GLN | ILE | TYR | GLU | GLU | ALA | ARG | LYS | PHE | ||||
17 | SER | TYR | ARG | SER | ARG | VAL | ARG | PRO | CYS | VAL | ||||
18 | VAL | TYR | GLY | GLY | ALA | ASP | ILE | GLY | GLN | GLN | ||||
19 | ILE | ARG | ASP | LEU | GLU | ARG | GLY | CYS | HIS | LEU | ||||
20 | LEU | VAL | ALA | THR | PRO | GLY | ARG | LEU | VAL | ASP | ||||
21 | MET | MET | GLU | ARG | GLY | LYS | ILE | GLY | LEU | ASP | ||||
22 | PHE | CYS | LYS | TYR | LEU | VAL | LEU | ASP | GLU | ALA | ||||
23 | ASP | ARG | MET | LEU | ASP | MET | GLY | PHE | GLU | PRO | ||||
24 | GLN | ILE | ARG | ARG | ILE | VAL | GLU | GLN | ASP | THR | ||||
25 | MET | PRO | PRO | LYS | GLY | VAL | ARG | HIS | THR | MET | ||||
26 | MET | PHE | SER | ALA | THR | PHE | PRO | LYS | GLU | ILE | ||||
27 | GLN | MET | LEU | ALA | ARG | ASP | PHE | LEU | ASP | GLU | ||||
28 | TYR | ILE | PHE | LEU | ALA | VAL | GLY | ARG | VAL |
Samples:
sample_1: D1 domain, [U-2H, 13C, 15N; Iled1-13C1H3; Leud/Valg-13C1H3/12CD3], 1.4 mM; MES 20 mM; sodium chloride 150 mM; DTT 5 mM
sample_conditions_1: ionic strength: 170 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N TROSY | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HMCM(CG)CB | sample_1 | isotropic | sample_conditions_1 |
3D HMCM(CGCB)CA | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN - collection
NMRPipe - processing
NMRFAM-SPARKY - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE III 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts