BMRB Entry 51078
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51078
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Title: Backbone and side-chain resonance assignments of the harmonin homology domain 1 (HHD1) of human RTEL1 PubMed: 35320499
Deposition date: 2021-09-07 Original release date: 2022-05-06
Authors: Ghosh, Meenakshi; Kumar, Niranjan; Manikandan, Parthasarathy; Basak, Sanmoyee; Singh, Mahavir
Citation: Kumar, Niranjan; Ghosh, Meenakshi; Manikandan, Parthasarathy; Basak, Sanmoyee; Deepa, Akula; Singh, Mahavir. "Resonance assignment and secondary structure of the tandem harmonin homology domains of human RTEL1" Biomol. NMR Assign. 16, 159-164 (2022).
Assembly members:
entity_1, polymer, 104 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: pET28a
Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSEPVAGAQTD
RAKLFMVAVKQELSQANFAT
FTQALQDYKGSDDFAALAAC
LGPLFAEDPKKHNLLQGFYQ
FVRPHHKQQFEEVCIQLTGR
GCGY
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 316 |
| 15N chemical shifts | 92 |
| 1H chemical shifts | 498 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RTEL1_HHD1 | 1 |
Entities:
Entity 1, RTEL1_HHD1 104 residues - Formula weight is not available
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | GLU | PRO | VAL | ALA | GLY | ALA | GLN | THR | ASP | ||||
| 3 | ARG | ALA | LYS | LEU | PHE | MET | VAL | ALA | VAL | LYS | ||||
| 4 | GLN | GLU | LEU | SER | GLN | ALA | ASN | PHE | ALA | THR | ||||
| 5 | PHE | THR | GLN | ALA | LEU | GLN | ASP | TYR | LYS | GLY | ||||
| 6 | SER | ASP | ASP | PHE | ALA | ALA | LEU | ALA | ALA | CYS | ||||
| 7 | LEU | GLY | PRO | LEU | PHE | ALA | GLU | ASP | PRO | LYS | ||||
| 8 | LYS | HIS | ASN | LEU | LEU | GLN | GLY | PHE | TYR | GLN | ||||
| 9 | PHE | VAL | ARG | PRO | HIS | HIS | LYS | GLN | GLN | PHE | ||||
| 10 | GLU | GLU | VAL | CYS | ILE | GLN | LEU | THR | GLY | ARG | ||||
| 11 | GLY | CYS | GLY | TYR |
Samples:
sample_1: RTEL1_HHD1, [U-99% 13C; U-99% 15N], 0.7 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 2 mM; sodium azide 0.02%
sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | 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 HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
VNMRj - collection
NMRPipe - processing
CcpNMR - chemical shift assignment
NMR spectrometers:
- Agilent DRX 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts