BMRB Entry 52542
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52542
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Title: Backbone resonance assignemnts of HUWE1 HECT domain N-lobe
Deposition date: 2024-07-09 Original release date: 2024-07-16
Authors: Zhang, Haoran; Li, Yan
Citation: Zhang, Haoran; Li, Yan. "Backbone resonance assignemnts of HUWE1 HECT domain N-lobe" .
Assembly members:
entity_1, polymer, 266 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: pET-28a
Entity Sequences (FASTA):
entity_1: GPGSDFDVKRKYFRQELERL
DEGLRKEDMAVHVRRDHVFE
DSYRELHRKSPEEMKNRLYI
VFEGEEGQDAGGLLREWYMI
ISREMFNPMYALFRTSPGDR
VTYTINPSSHCNPNHLSYFK
FVGRIVAKAVYDNRLLECYF
TRSFYKHILGKSVRYTDMES
EDYHFYQGLVYLLENDVSTL
GYDLTFSTEVQEFGVCEVRD
LKPNGANILVTEENKKEYVH
LVCQMRMTGAIRKQLAAFLE
GFYEIIPKRLISIFTEQELE
LLISGL
| Data type | Count |
| 13C chemical shifts | 645 |
| 15N chemical shifts | 215 |
| 1H chemical shifts | 215 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HUWE1 HECT domain N-lobe | 1 |
Entities:
Entity 1, HUWE1 HECT domain N-lobe 266 residues - Formula weight is not available
| 1 | GLY | PRO | GLY | SER | ASP | PHE | ASP | VAL | LYS | ARG | ||||
| 2 | LYS | TYR | PHE | ARG | GLN | GLU | LEU | GLU | ARG | LEU | ||||
| 3 | ASP | GLU | GLY | LEU | ARG | LYS | GLU | ASP | MET | ALA | ||||
| 4 | VAL | HIS | VAL | ARG | ARG | ASP | HIS | VAL | PHE | GLU | ||||
| 5 | ASP | SER | TYR | ARG | GLU | LEU | HIS | ARG | LYS | SER | ||||
| 6 | PRO | GLU | GLU | MET | LYS | ASN | ARG | LEU | TYR | ILE | ||||
| 7 | VAL | PHE | GLU | GLY | GLU | GLU | GLY | GLN | ASP | ALA | ||||
| 8 | GLY | GLY | LEU | LEU | ARG | GLU | TRP | TYR | MET | ILE | ||||
| 9 | ILE | SER | ARG | GLU | MET | PHE | ASN | PRO | MET | TYR | ||||
| 10 | ALA | LEU | PHE | ARG | THR | SER | PRO | GLY | ASP | ARG | ||||
| 11 | VAL | THR | TYR | THR | ILE | ASN | PRO | SER | SER | HIS | ||||
| 12 | CYS | ASN | PRO | ASN | HIS | LEU | SER | TYR | PHE | LYS | ||||
| 13 | PHE | VAL | GLY | ARG | ILE | VAL | ALA | LYS | ALA | VAL | ||||
| 14 | TYR | ASP | ASN | ARG | LEU | LEU | GLU | CYS | TYR | PHE | ||||
| 15 | THR | ARG | SER | PHE | TYR | LYS | HIS | ILE | LEU | GLY | ||||
| 16 | LYS | SER | VAL | ARG | TYR | THR | ASP | MET | GLU | SER | ||||
| 17 | GLU | ASP | TYR | HIS | PHE | TYR | GLN | GLY | LEU | VAL | ||||
| 18 | TYR | LEU | LEU | GLU | ASN | ASP | VAL | SER | THR | LEU | ||||
| 19 | GLY | TYR | ASP | LEU | THR | PHE | SER | THR | GLU | VAL | ||||
| 20 | GLN | GLU | PHE | GLY | VAL | CYS | GLU | VAL | ARG | ASP | ||||
| 21 | LEU | LYS | PRO | ASN | GLY | ALA | ASN | ILE | LEU | VAL | ||||
| 22 | THR | GLU | GLU | ASN | LYS | LYS | GLU | TYR | VAL | HIS | ||||
| 23 | LEU | VAL | CYS | GLN | MET | ARG | MET | THR | GLY | ALA | ||||
| 24 | ILE | ARG | LYS | GLN | LEU | ALA | ALA | PHE | LEU | GLU | ||||
| 25 | GLY | PHE | TYR | GLU | ILE | ILE | PRO | LYS | ARG | LEU | ||||
| 26 | ILE | SER | ILE | PHE | THR | GLU | GLN | GLU | LEU | GLU | ||||
| 27 | LEU | LEU | ILE | SER | GLY | LEU |
Samples:
sample_1: HUWE1 HECT domain N-lobe, [U-13C; U-15N; U-2H], 400 uM; D2O, [U-100% 2H], 5 % v/v; sodium chloride 200 mM; TRIS 20 mM; TCEP 2 mM
sample_conditions_1: ionic strength: 222.4 mM; pH: 8.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | 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 HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
Software:
VNMR - collection
NMRPipe - processing
POKY - chemical shift assignment, data analysis, peak picking
NMR spectrometers:
- Varian VNMRS 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts