BMRB Entry 16613
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16613
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Title: SARS Coronavirus-unique domain (SUD): Three-domain molecular architecture in solution and RNA binding PubMed: 20493876
Deposition date: 2009-11-19 Original release date: 2010-06-15
Authors: Johnson, Margaret; Chatterjee, Amarnath; Wuthrich, Kurt
Citation: Johnson, Margaret; Chatterjee, Amarnath; Neuman, Benjamin; Wuthrich, Kurt. "SARS coronavirus unique domain: three-domain molecular architecture in solution and RNA binding." J. Mol. Biol. 400, 724-742 (2010).
Assembly members:
SUD-MC, polymer, 198 residues, Formula weight is not available
Natural source: Common Name: SARS coronavirus Taxonomy ID: 227859 Superkingdom: Viruses Kingdom: not available Genus/species: Coronavirus SARS coronavirus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
SUD-MC: GSHMGTVSWNLREMLAHAEE
TRKLMPICMDVRAIMATIQR
KYKGIKIQEGIVDYGVRFFF
YTSKEPVASIITKLNSLNEP
LVTMPIGYVTHGFNLEEAAR
CMRSLKAPAVVSVSSPDAVT
TYNGYLTSSSKTSEEHFVET
VSLAGSYRDWSYSGQRTELG
VEFLKRGDKIVYHTLESPVE
FHLDGEVLSLDKLKSLLS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 675 |
| 15N chemical shifts | 201 |
| 1H chemical shifts | 1407 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SUD-MC | 1 |
Entities:
Entity 1, SUD-MC 198 residues - Formula weight is not available
Residues 1-4 represent a vector-derived tag. Residues 5-198 represent two domains of a multidomain protein. Residue 178 (PRO 700) is in cis conformation.
| 1 | GLY | SER | HIS | MET | GLY | THR | VAL | SER | TRP | ASN | ||||
| 2 | LEU | ARG | GLU | MET | LEU | ALA | HIS | ALA | GLU | GLU | ||||
| 3 | THR | ARG | LYS | LEU | MET | PRO | ILE | CYS | MET | ASP | ||||
| 4 | VAL | ARG | ALA | ILE | MET | ALA | THR | ILE | GLN | ARG | ||||
| 5 | LYS | TYR | LYS | GLY | ILE | LYS | ILE | GLN | GLU | GLY | ||||
| 6 | ILE | VAL | ASP | TYR | GLY | VAL | ARG | PHE | PHE | PHE | ||||
| 7 | TYR | THR | SER | LYS | GLU | PRO | VAL | ALA | SER | ILE | ||||
| 8 | ILE | THR | LYS | LEU | ASN | SER | LEU | ASN | GLU | PRO | ||||
| 9 | LEU | VAL | THR | MET | PRO | ILE | GLY | TYR | VAL | THR | ||||
| 10 | HIS | GLY | PHE | ASN | LEU | GLU | GLU | ALA | ALA | ARG | ||||
| 11 | CYS | MET | ARG | SER | LEU | LYS | ALA | PRO | ALA | VAL | ||||
| 12 | VAL | SER | VAL | SER | SER | PRO | ASP | ALA | VAL | THR | ||||
| 13 | THR | TYR | ASN | GLY | TYR | LEU | THR | SER | SER | SER | ||||
| 14 | LYS | THR | SER | GLU | GLU | HIS | PHE | VAL | GLU | THR | ||||
| 15 | VAL | SER | LEU | ALA | GLY | SER | TYR | ARG | ASP | TRP | ||||
| 16 | SER | TYR | SER | GLY | GLN | ARG | THR | GLU | LEU | GLY | ||||
| 17 | VAL | GLU | PHE | LEU | LYS | ARG | GLY | ASP | LYS | ILE | ||||
| 18 | VAL | TYR | HIS | THR | LEU | GLU | SER | PRO | VAL | GLU | ||||
| 19 | PHE | HIS | LEU | ASP | GLY | GLU | VAL | LEU | SER | LEU | ||||
| 20 | ASP | LYS | LEU | LYS | SER | LEU | LEU | SER |
Samples:
sample_1: SUD-MC, [U-98% 13C; U-98% 15N], 1.0 mM; sodium phosphate 25 mM; sodium chloride 150 mM; sodium azide 2 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.227 M; pH: 6.8; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D [15N,1H]-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D [13C,1H]-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 15N-resolved [1H,1H-NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D aliphatic 13C-resolved [1H,1H]-NOESY | sample_1 | isotropic | sample_conditions_1 |
| 4D APSY-HACANH | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY-CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY-HACACONH | sample_1 | isotropic | sample_conditions_1 |
| 4D APSY-HNCOCA | sample_1 | isotropic | sample_conditions_1 |
| 3D aromatic 13C-resolved [1H,1H]-NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
CARA, Keller and Wuthrich - chemical shift assignment
ASCAN, Fiorito F, Herrmann T, Damberger FF, Wuthrich K. - chemical shift assignment
MATCH, Volk, J., Herrmann, T., Wuthrich, K - chemical shift assignment
ATNOS, Herrmann T, Guntert P, Wuthrich K - peak picking
CANDID, Herrmann T, Guntert P, Wuthrich K - structure solution
OpalP, Luginbuhl P, Guntert P, Billeter M, Wuthrich K. - refinement
UNIO, Herrmann T, Wuthrich K - structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| BMRB | 15469 15618 |
| PDB | |
| DBJ | BAC81346 BAC81347 BAC81360 BAC81361 BAC81374 |
| GB | AAP13439 AAP13442 AAP13566 AAP13575 AAP30028 |
| REF | NP_828849 NP_828850 NP_828862 |
| SP | P0C6U8 P0C6X7 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts