BMRB Entry 30569
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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/BMR30569
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Title: Structure of the C-terminal Helical Repeat Domain of Eukaryotic Elongation Factor 2 Kinase (eEF-2K) PubMed: 31108082
Deposition date: 2019-02-08 Original release date: 2019-05-24
Authors: Piserchio, A.; Will, N.; Giles, D.; Hajredini, F.; Dalby, K.; Ghose, R.
Citation: Piserchio, A.; Will, N.; Giles, D.; Hajredini, F.; Dalby, K.; Ghose, R.. "Solution Structure of the Carboxy-Terminal Tandem Repeat Domain of Eukaryotic Elongation Factor 2 Kinase and its Role in Substrate Recognition." J. Mol. Biol. 431, 2700-2717 (2019).
Assembly members:
entity_1, polymer, 167 residues, 18893.021 Da.
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 BL21(DE3)
Entity Sequences (FASTA):
entity_1: SHMGELEAIVGLGLMYSQLP
HHILADVSLKETEENKTKGF
DYLLKAAEAGDRQSMILVAR
AFDSGQNLSPDRCQDWLEAL
HWYNTALEMTDCDEGGEYDG
MQDEPRYMMLAREAEMLFTG
GYGLEKDPQRSGDLYTQAAE
AAMEAMKGRLANQYYQKAEE
AWAQMEE
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 712 |
| 15N chemical shifts | 183 |
| 1H chemical shifts | 1124 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 167 residues - 18893.021 Da.
| 1 | SER | HIS | MET | GLY | GLU | LEU | GLU | ALA | ILE | VAL | ||||
| 2 | GLY | LEU | GLY | LEU | MET | TYR | SER | GLN | LEU | PRO | ||||
| 3 | HIS | HIS | ILE | LEU | ALA | ASP | VAL | SER | LEU | LYS | ||||
| 4 | GLU | THR | GLU | GLU | ASN | LYS | THR | LYS | GLY | PHE | ||||
| 5 | ASP | TYR | LEU | LEU | LYS | ALA | ALA | GLU | ALA | GLY | ||||
| 6 | ASP | ARG | GLN | SER | MET | ILE | LEU | VAL | ALA | ARG | ||||
| 7 | ALA | PHE | ASP | SER | GLY | GLN | ASN | LEU | SER | PRO | ||||
| 8 | ASP | ARG | CYS | GLN | ASP | TRP | LEU | GLU | ALA | LEU | ||||
| 9 | HIS | TRP | TYR | ASN | THR | ALA | LEU | GLU | MET | THR | ||||
| 10 | ASP | CYS | ASP | GLU | GLY | GLY | GLU | TYR | ASP | GLY | ||||
| 11 | MET | GLN | ASP | GLU | PRO | ARG | TYR | MET | MET | LEU | ||||
| 12 | ALA | ARG | GLU | ALA | GLU | MET | LEU | PHE | THR | GLY | ||||
| 13 | GLY | TYR | GLY | LEU | GLU | LYS | ASP | PRO | GLN | ARG | ||||
| 14 | SER | GLY | ASP | LEU | TYR | THR | GLN | ALA | ALA | GLU | ||||
| 15 | ALA | ALA | MET | GLU | ALA | MET | LYS | GLY | ARG | LEU | ||||
| 16 | ALA | ASN | GLN | TYR | TYR | GLN | LYS | ALA | GLU | GLU | ||||
| 17 | ALA | TRP | ALA | GLN | MET | GLU | GLU |
Samples:
sample_1: eEF2K (562-725), [U-99% 13C; U-99% 15N], 200 ± 20 uM; sodium phosphate 20 ± 1 mM; sodium chloride 100 ± 5 mM; DTT 4 ± 0.4 mM; EDTA 0.2 ± 0.02 mM; AEBSF protease inhibitor 2 ± 0.02 mM
sample_2: eEF2K (562-725), [U-99% 13C; U-99% 15N], 400 ± 40 uM; sodium phosphate 20 ± 1 mM; sodium chloride 100 ± 5 mM; DTT 4 ± 0.4 mM; EDTA 0.2 ± 0.02 mM; AEBSF protease inhibitor 2 ± 0.02 mM
sample_3: eEF2K (562-725), [U-99% 13C; U-99% 15N], 340 ± 35 uM; sodium phosphate 14 ± 2 mM; sodium chloride 100 ± 5 mM; DTT 4 ± 0.4 mM; EDTA 0.2 ± 0.02 mM; AEBSF protease inhibitor 2 ± 0.2 mM; Pf1 phage 14 ± 2 mg/mL
sample_4: eEF2K (562-725), [U-99% 13C; U-99% 15N], 360 ± 36 uM; sodium phosphate 20 ± 1 mM; sodium chloride 100 ± 5 mM; DTT 4 ± 0.4 mM; EDTA 0.2 ± 0.02 mM; AEBSF protease inhibitor 2 ± 0.02 mM
sample_conditions_1: ionic strength: 120 mM; pH: 6.5; pressure: 1 atm; temperature: 298.15 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 4D HC-HSQC-NOESY-HN-HSQC | sample_4 | isotropic | sample_conditions_1 |
| 3D 3D NNH (15N-HSQC-NOESY-15N-HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_4 | isotropic | sample_conditions_1 |
| 3D H-13C NOESY aromatic | sample_4 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_2 | isotropic | sample_conditions_1 |
| 3D Hcc(co)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D hCc(co)NH | sample_2 | anisotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 15N HSQC-IPAP | sample_3 | anisotropic | sample_conditions_1 |
| 3D IPAP-J-HNCO | sample_3 | anisotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SMILE, Ying, J., Delaglio, F., Torchia, D. A. & Bax, A. - processing
NMRView, Johnson, One Moon Scientific - data analysis, peak picking
TALOSN, Shen, Y. & Bax, A. - data analysis
PALES, Zweckstetter, M - data analysis
ARIA, Linge, O'Donoghue and Nilges - structure calculation
NMR spectrometers:
- Bruker Avance 900 MHz
- Bruker Avance 800 MHz
- Bruker AVANCE III 800 MHz
- Bruker AVANCE III 700 MHz
- Bruker AVANCE III 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts