BMRB Entry 51211
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51211
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Title: 13C/15N/1H chemical shift assignments for Human Cytomegalovirus Protease delta221 PubMed: 35364007
Deposition date: 2021-12-03 Original release date: 2022-04-07
Authors: Lee, Gregory; Craik, Charles
Citation: Hulce, Kaitlin; Jaishankar, Priyadarshini; Lee, Gregory; Bohn, Markus-Frederik; Connelly, Emily; Wucherer, Kristin; Volk, Regan; Chuo, Shih-Wei; Arkin, Michelle; Renslo, Adam; Craik, Charles. "Inhibiting a dynamic viral protease by targeting a non-catalytic cysteine" Cell Chem. Biol. 29, 785-798 (2022).
Assembly members:
entity_1, polymer, 228 residues, 24033.9 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 Vector: pET21b
Entity Sequences (FASTA):
entity_1: MHHHHHHMTMDEQQSQAVAP
VYVGGFLARYDQSPDEAELL
LPRDVVEHWLHAQGQGQPSL
SVALPLNINHDDTAVVGHVA
AMQSVRDGLFCLGCVTSPRF
LEIVRRASEKSELVSRGPVS
PLQPDKVVEFLSGSYAGLSL
SSRRCDDVEVATSLSGSETT
PFKHVALCSVGRRRGTLAVY
GRDPEWVTQRFPDLTAADRD
GLRAQWQRCGSTAVDVSGDP
FRSDSYGL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 695 |
| 15N chemical shifts | 203 |
| 1H chemical shifts | 592 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HCMV Pr delta221 | 1 |
Entities:
Entity 1, HCMV Pr delta221 228 residues - 24033.9 Da.
Contains a non-native N-terminal Met+His6-tag (residues -7 to -1). Residue numbering begins at Met1. This is a C-terminal truncated construct that ends with L221.
| 1 | MET | HIS | HIS | HIS | HIS | HIS | HIS | MET | THR | MET | ||||
| 2 | ASP | GLU | GLN | GLN | SER | GLN | ALA | VAL | ALA | PRO | ||||
| 3 | VAL | TYR | VAL | GLY | GLY | PHE | LEU | ALA | ARG | TYR | ||||
| 4 | ASP | GLN | SER | PRO | ASP | GLU | ALA | GLU | LEU | LEU | ||||
| 5 | LEU | PRO | ARG | ASP | VAL | VAL | GLU | HIS | TRP | LEU | ||||
| 6 | HIS | ALA | GLN | GLY | GLN | GLY | GLN | PRO | SER | LEU | ||||
| 7 | SER | VAL | ALA | LEU | PRO | LEU | ASN | ILE | ASN | HIS | ||||
| 8 | ASP | ASP | THR | ALA | VAL | VAL | GLY | HIS | VAL | ALA | ||||
| 9 | ALA | MET | GLN | SER | VAL | ARG | ASP | GLY | LEU | PHE | ||||
| 10 | CYS | LEU | GLY | CYS | VAL | THR | SER | PRO | ARG | PHE | ||||
| 11 | LEU | GLU | ILE | VAL | ARG | ARG | ALA | SER | GLU | LYS | ||||
| 12 | SER | GLU | LEU | VAL | SER | ARG | GLY | PRO | VAL | SER | ||||
| 13 | PRO | LEU | GLN | PRO | ASP | LYS | VAL | VAL | GLU | PHE | ||||
| 14 | LEU | SER | GLY | SER | TYR | ALA | GLY | LEU | SER | LEU | ||||
| 15 | SER | SER | ARG | ARG | CYS | ASP | ASP | VAL | GLU | VAL | ||||
| 16 | ALA | THR | SER | LEU | SER | GLY | SER | GLU | THR | THR | ||||
| 17 | PRO | PHE | LYS | HIS | VAL | ALA | LEU | CYS | SER | VAL | ||||
| 18 | GLY | ARG | ARG | ARG | GLY | THR | LEU | ALA | VAL | TYR | ||||
| 19 | GLY | ARG | ASP | PRO | GLU | TRP | VAL | THR | GLN | ARG | ||||
| 20 | PHE | PRO | ASP | LEU | THR | ALA | ALA | ASP | ARG | ASP | ||||
| 21 | GLY | LEU | ARG | ALA | GLN | TRP | GLN | ARG | CYS | GLY | ||||
| 22 | SER | THR | ALA | VAL | ASP | VAL | SER | GLY | ASP | PRO | ||||
| 23 | PHE | ARG | SER | ASP | SER | TYR | GLY | LEU |
Samples:
sample_1: HCMV Protease delta 221, [U-13C; U-15N; U-2H], 150 uM; potassium phosphate 25 mM; potassium chloride 150 mM; D2O, [U-100% 2H], 10%; DTT 1 mM; EDTA 0.5 mM
sample_2: HCMV Protease delta 221, [U-100% 13C; U-100% 15N], 150 uM; potassium phosphate 25 mM; potassium chloride 150 mM; D2O, [U-100% 2H], 10%; DTT 1 mM; EDTA 0.5 mM
sample_3: HCMV Protease delta 221, [U-100% 15N], 150 uM; potassium phosphate 25 mM; potassium chloride 150 mM; D2O, [U-100% 2H], 10%; DTT 1 mM; EDTA 0.5 mM
sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 300 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_2 | 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 CC(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_3 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v1.3pl10 v1.3pl10 - collection
TOPSPIN v2.1pl8 v2.1pl8 - collection
NMRPipe v8.7 v8.7 - processing
SPARKY v.3.114 v3.114 - chemical shift assignment, data analysis, peak picking
NMR spectrometers:
- Bruker Avance/DRX 500 MHz
- Bruker Avance 800 MHz
Related Database Links:
| NCBI | 2554902 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts