BMRB Entry 17251
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17251
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Title: the N-terminal domain of SARS-CoV main protease PubMed: 21181312
Deposition date: 2010-10-12 Original release date: 2011-01-18
Authors: Zhang, Shengnan; Zhong, Nan; Ren, Xiaobai; Jin, Changwen; Xia, Bin
Citation: Zhang, Shengnan; Zhong, Nan; Ren, Xiaobai; Jin, Changwen; Xia, Bin. "1H, 13C and 15N resonance assignments of SARS-CoV main protease N-terminal domain." Biomol. NMR Assignments 5, 143-145 (2011).
Assembly members:
main_protease_N-terminal_domain, polymer, 199 residues, Formula weight is not available
Natural source: Common Name: SARS coronavirus Taxonomy ID: 227859 Superkingdom: virus Kingdom: not available Genus/species: Betacoronavirus Severe acute respiratory syndrome-related coronavirus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
main_protease_N-terminal_domain: SGFRKMAFPSGKVEGCMVQV
TCGTTTLNGLWLDDTVYCPR
HVICTAEDMLNPNYEDLLIR
KSNHSFLVQAGNVQLRVIGH
SMQNCLLRLKVDTSNPKTPK
YKFVRIQPGQTFSVLACYNG
SPSGVYQCAMRPNHTIKGSF
LNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGK
FYGPFVDRQTAQAAGTDTT
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 762 |
| 15N chemical shifts | 198 |
| 1H chemical shifts | 1225 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SARS-CoV main protease N-terminal domain | 1 |
Entities:
Entity 1, SARS-CoV main protease N-terminal domain 199 residues - Formula weight is not available
| 1 | SER | GLY | PHE | ARG | LYS | MET | ALA | PHE | PRO | SER | ||||
| 2 | GLY | LYS | VAL | GLU | GLY | CYS | MET | VAL | GLN | VAL | ||||
| 3 | THR | CYS | GLY | THR | THR | THR | LEU | ASN | GLY | LEU | ||||
| 4 | TRP | LEU | ASP | ASP | THR | VAL | TYR | CYS | PRO | ARG | ||||
| 5 | HIS | VAL | ILE | CYS | THR | ALA | GLU | ASP | MET | LEU | ||||
| 6 | ASN | PRO | ASN | TYR | GLU | ASP | LEU | LEU | ILE | ARG | ||||
| 7 | LYS | SER | ASN | HIS | SER | PHE | LEU | VAL | GLN | ALA | ||||
| 8 | GLY | ASN | VAL | GLN | LEU | ARG | VAL | ILE | GLY | HIS | ||||
| 9 | SER | MET | GLN | ASN | CYS | LEU | LEU | ARG | LEU | LYS | ||||
| 10 | VAL | ASP | THR | SER | ASN | PRO | LYS | THR | PRO | LYS | ||||
| 11 | TYR | LYS | PHE | VAL | ARG | ILE | GLN | PRO | GLY | GLN | ||||
| 12 | THR | PHE | SER | VAL | LEU | ALA | CYS | TYR | ASN | GLY | ||||
| 13 | SER | PRO | SER | GLY | VAL | TYR | GLN | CYS | ALA | MET | ||||
| 14 | ARG | PRO | ASN | HIS | THR | ILE | LYS | GLY | SER | PHE | ||||
| 15 | LEU | ASN | GLY | SER | CYS | GLY | SER | VAL | GLY | PHE | ||||
| 16 | ASN | ILE | ASP | TYR | ASP | CYS | VAL | SER | PHE | CYS | ||||
| 17 | TYR | MET | HIS | HIS | MET | GLU | LEU | PRO | THR | GLY | ||||
| 18 | VAL | HIS | ALA | GLY | THR | ASP | LEU | GLU | GLY | LYS | ||||
| 19 | PHE | TYR | GLY | PRO | PHE | VAL | ASP | ARG | GLN | THR | ||||
| 20 | ALA | GLN | ALA | ALA | GLY | THR | ASP | THR | THR |
Samples:
sample_1: main protease N-terminal domain, [U-13C; U-15N], 0.7 mM; potassium phosphate 50 mM; sodium chloride 50 mM; Argine 30 mM; Glutamine acid 30 mM; EDTA 1 mM; DTT 10 mM; D2O 10%; H2O 90%; sodium azide 0.05 w/v; DSS 0.02 w/v
sample_conditions_1: ionic strength: 170 mM; pH: 7.0; pressure: 1 atm; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - data analysis
xwinnmr, Bruker Biospin - collection
TOPSPIN, Bruker Biospin - collection
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAC81346 BAC81347 BAC81360 BAC81361 BAC81374 |
| GB | AAP13439 AAP13442 AAP13566 AAP13575 AAP30028 |
| REF | NP_828849 NP_828850 NP_828863 |
| SP | P0C6F5 P0C6F8 P0C6T7 P0C6U8 P0C6V9 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts