BMRB Entry 51711
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51711
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Title: 1H, 13C, 15N backbone chemical shift assignments for DDX4 1-236 PubMed: 37980572
Deposition date: 2022-11-28 Original release date: 2023-11-20
Authors: Crabtree, Michael; Redfield, Christina; Nott, Tim
Citation: Crabtree, Michael; Holland, Jack; Pillai, Arvind; Kompella, Purnima; Babl, Leon; Turner, Noah; Eaton, James; Hochberg, Georg; Aarts, Dirk; Redfield, Christina; Baldwin, Andrew; Nott, Timothy. "Ion binding with charge inversion combined with screening modulates DEAD box helicase phase transitions" Cell Rep. 42, 113375-113375 (2023).
Assembly members:
entity_1, polymer, 236 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: modified pETM-30 containing pGEX-2T-TEV site and pProEx multiple cloning sites
Entity Sequences (FASTA):
entity_1: MGDEDWEAEINPHMSSYVPI
FEKDRYSGENGDNFNRTPAS
SSEMDDGPSRRDHFMKSGFA
SGRNFGNRDAGECNKRDNTS
TMGGFGVGKSFGNRGFSNSR
FEDGDSSGFWRESSNDCEDN
PTRNRGFSKRGGYRDGNNSE
ASGPYRRGGRGSFRGCRGGF
GLGSPNNDLDPDECMQRTGG
LFGSRRPVLSGTGNGDTSQS
RSGSGSERGGYKGLNEEVIT
GSGKNSWKSEAEGGES
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 511 |
| 15N chemical shifts | 185 |
| 1H chemical shifts | 185 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | DDX4 | 1 |
Entities:
Entity 1, DDX4 236 residues - Formula weight is not available
| 1 | MET | GLY | ASP | GLU | ASP | TRP | GLU | ALA | GLU | ILE | ||||
| 2 | ASN | PRO | HIS | MET | SER | SER | TYR | VAL | PRO | ILE | ||||
| 3 | PHE | GLU | LYS | ASP | ARG | TYR | SER | GLY | GLU | ASN | ||||
| 4 | GLY | ASP | ASN | PHE | ASN | ARG | THR | PRO | ALA | SER | ||||
| 5 | SER | SER | GLU | MET | ASP | ASP | GLY | PRO | SER | ARG | ||||
| 6 | ARG | ASP | HIS | PHE | MET | LYS | SER | GLY | PHE | ALA | ||||
| 7 | SER | GLY | ARG | ASN | PHE | GLY | ASN | ARG | ASP | ALA | ||||
| 8 | GLY | GLU | CYS | ASN | LYS | ARG | ASP | ASN | THR | SER | ||||
| 9 | THR | MET | GLY | GLY | PHE | GLY | VAL | GLY | LYS | SER | ||||
| 10 | PHE | GLY | ASN | ARG | GLY | PHE | SER | ASN | SER | ARG | ||||
| 11 | PHE | GLU | ASP | GLY | ASP | SER | SER | GLY | PHE | TRP | ||||
| 12 | ARG | GLU | SER | SER | ASN | ASP | CYS | GLU | ASP | ASN | ||||
| 13 | PRO | THR | ARG | ASN | ARG | GLY | PHE | SER | LYS | ARG | ||||
| 14 | GLY | GLY | TYR | ARG | ASP | GLY | ASN | ASN | SER | GLU | ||||
| 15 | ALA | SER | GLY | PRO | TYR | ARG | ARG | GLY | GLY | ARG | ||||
| 16 | GLY | SER | PHE | ARG | GLY | CYS | ARG | GLY | GLY | PHE | ||||
| 17 | GLY | LEU | GLY | SER | PRO | ASN | ASN | ASP | LEU | ASP | ||||
| 18 | PRO | ASP | GLU | CYS | MET | GLN | ARG | THR | GLY | GLY | ||||
| 19 | LEU | PHE | GLY | SER | ARG | ARG | PRO | VAL | LEU | SER | ||||
| 20 | GLY | THR | GLY | ASN | GLY | ASP | THR | SER | GLN | SER | ||||
| 21 | ARG | SER | GLY | SER | GLY | SER | GLU | ARG | GLY | GLY | ||||
| 22 | TYR | LYS | GLY | LEU | ASN | GLU | GLU | VAL | ILE | THR | ||||
| 23 | GLY | SER | GLY | LYS | ASN | SER | TRP | LYS | SER | GLU | ||||
| 24 | ALA | GLU | GLY | GLY | GLU | SER |
Samples:
sample_1: DDX4, [U-99% 13C; U-99% 15N], 44.6 uM; TCEP 5 mM; PIPES 20 mM; sodium chloride 138.5 mM; D2O, [U-99% 2H], 5%
sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N BEST-TROSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N BEST-TROSY | sample_1 | isotropic | sample_conditions_1 |
| 3D BEST-TROSY-HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D BEST-TROSY-HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D BEST-TROSY-HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
| 3D BEST-TROSY-HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D BEST-TROSY-HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CC(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)NNH | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(COCA)NNH | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.2 - collection
CcpNMR v2.5 - chemical shift assignment, data analysis
NMRPipe v9.7 - processing
istHMS vV211 - processing
NMR spectrometers:
- Bruker AVANCE III 750 MHz
- Bruker AVANCE III 950 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts