BMRB Entry 17911
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17911
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Title: C-terminal domain of SARS-CoV main protease
Deposition date: 2011-09-02 Original release date: 2012-09-04
Authors: Xia, Bin; Kang, Xue
Citation: Xia, Bin. "NMR solution structure of C-terminal domain of SARS-CoV main protease in 2.5M urea" Not known ., .-..
Assembly members:
Mpro-C, polymer, 120 residues, Formula weight is not available
Natural source: Common Name: SARS coronavirus Taxonomy ID: 227859 Superkingdom: Viruses Kingdom: not available Genus/species: SARS coronavirus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Mpro-C: DRQTAQAAGTDTTITLNVLA
WLYAAVINGDRWFLNRFTTT
LNDFNLVAMKYNYEPLTQDH
VDILGPLSAQTGIAVLDMCA
ALKELLQNGMNGRTILGSTI
LEDEFTPFDVVRQCSGVTFQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 360 |
| 15N chemical shifts | 130 |
| 1H chemical shifts | 795 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Mpro-C | 1 |
Entities:
Entity 1, Mpro-C 120 residues - Formula weight is not available
| 1 | ASP | ARG | GLN | THR | ALA | GLN | ALA | ALA | GLY | THR | |
| 2 | ASP | THR | THR | ILE | THR | LEU | ASN | VAL | LEU | ALA | |
| 3 | TRP | LEU | TYR | ALA | ALA | VAL | ILE | ASN | GLY | ASP | |
| 4 | ARG | TRP | PHE | LEU | ASN | ARG | PHE | THR | THR | THR | |
| 5 | LEU | ASN | ASP | PHE | ASN | LEU | VAL | ALA | MET | LYS | |
| 6 | TYR | ASN | TYR | GLU | PRO | LEU | THR | GLN | ASP | HIS | |
| 7 | VAL | ASP | ILE | LEU | GLY | PRO | LEU | SER | ALA | GLN | |
| 8 | THR | GLY | ILE | ALA | VAL | LEU | ASP | MET | CYS | ALA | |
| 9 | ALA | LEU | LYS | GLU | LEU | LEU | GLN | ASN | GLY | MET | |
| 10 | ASN | GLY | ARG | THR | ILE | LEU | GLY | SER | THR | ILE | |
| 11 | LEU | GLU | ASP | GLU | PHE | THR | PRO | PHE | ASP | VAL | |
| 12 | VAL | ARG | GLN | CYS | SER | GLY | VAL | THR | PHE | GLN |
Samples:
sample_1: Mpro-C, [U-100% 15N], 1 mM; Mpro-C, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%; DTT 1 mM; PBS 50 mM
sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 298 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 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 HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - structure solution
NMRView, Johnson, One Moon Scientific - chemical shift assignment
ProcheckNMR, Laskowski and MacArthur - processing
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
SANE, Duggan, Legge, Dyson & Wright - structure solution
TALOS, Cornilescu, Delaglio and Bax - structure solution
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 800 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