BMRB Entry 51952
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51952
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Mondal, Somnath; Rousseau, Sabrina; Talenton, Vincent; Thiam, Cheikh Ahmadou Bamba; Aznauryan, Mikayel; Mackereth, Cameron. "Backbone resonance assignments of the C-terminal region of human translation initiation factor eIF4B" Biomol. NMR Assign. 17, 199-203 (2023).
PubMed: 37368134
Assembly members:
entity_1, polymer, 127 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: 2B-T
Entity Sequences (FASTA):
entity_1: GCKLNLKPRSTPKEDDSSAS
TSQSTRAASIFGGAKPVDTA
AREREVEERLQKEQEKLQRQ
LDEPKLERRPRERHPSWRSE
ETQERERSRTGSESSQTGTS
TTSSRNARRRESEKSLENET
LNKEEDC
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 363 |
| 15N chemical shifts | 123 |
| 1H chemical shifts | 243 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | eIF4B-CTRN | 1 |
Entities:
Entity 1, eIF4B-CTRN 127 residues - Formula weight is not available
Gly-Cys- was added at the N-terminus
| 1 | GLY | CYS | LYS | LEU | ASN | LEU | LYS | PRO | ARG | SER | ||||
| 2 | THR | PRO | LYS | GLU | ASP | ASP | SER | SER | ALA | SER | ||||
| 3 | THR | SER | GLN | SER | THR | ARG | ALA | ALA | SER | ILE | ||||
| 4 | PHE | GLY | GLY | ALA | LYS | PRO | VAL | ASP | THR | ALA | ||||
| 5 | ALA | ARG | GLU | ARG | GLU | VAL | GLU | GLU | ARG | LEU | ||||
| 6 | GLN | LYS | GLU | GLN | GLU | LYS | LEU | GLN | ARG | GLN | ||||
| 7 | LEU | ASP | GLU | PRO | LYS | LEU | GLU | ARG | ARG | PRO | ||||
| 8 | ARG | GLU | ARG | HIS | PRO | SER | TRP | ARG | SER | GLU | ||||
| 9 | GLU | THR | GLN | GLU | ARG | GLU | ARG | SER | ARG | THR | ||||
| 10 | GLY | SER | GLU | SER | SER | GLN | THR | GLY | THR | SER | ||||
| 11 | THR | THR | SER | SER | ARG | ASN | ALA | ARG | ARG | ARG | ||||
| 12 | GLU | SER | GLU | LYS | SER | LEU | GLU | ASN | GLU | THR | ||||
| 13 | LEU | ASN | LYS | GLU | GLU | ASP | CYS |
Samples:
sample_1: CTRN, [U-100% 13C; U-100% 15N], 460 uM; sodium phosphate 20 mM; sodium chloride 150 mM; DTT 2 mM
sample_conditions_1: ionic strength: 170 mM; pH: 7.0; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1D 1H | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HA(CACO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D N(COCA)NNH | sample_1 | isotropic | sample_conditions_1 |
| 3D HACAN | sample_1 | isotropic | sample_conditions_1 |
| 3D HACA(CO)N | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN - collection
NMRPipe - processing
NMRFAM-SPARKY - chemical shift assignment, data analysis
NMR spectrometers:
- Bruker AVANCE NEO 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks