BMRB Entry 15618
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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/BMR15618
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Title: NMR ASSIGNMENT OF THE DOMAIN 527-651 OF THE SARS-COV NONSTRUCTURAL PROTEIN NSP3 PubMed: 19052085
Deposition date: 2008-01-04 Original release date: 2008-01-30
Authors: Chatterjee, Amarnath; Johnson, Margaret; Serrano, Pedro; Pedrini, Bill; Joseph, Jeremiah; Saikatendu, Kumar; Neuman, Benjamin; Stevens, Raymond; Wilson, Ian; Buchmeier, Michael; Kuhn, Peter; Wuthrich, Kurt
Citation: Chatterjee, Amarnath; Johnson, Margaret; Serrano, Pedro; Pedrini, Bill; Joseph, Jeremiah; Neuman, Benjamin; Saikatendu, Kumar; Buchmeier, Michael; Kuhn, Peter; Wuthrich, Kurt. "Nuclear magnetic resonance structure shows that the severe acute respiratory syndrome coronavirus-unique domain contains a macrodomain fold" J. Virol. 83, 1823-1836 (2009).
Assembly members:
nsp3(527-651), polymer, 129 residues, Formula weight is not available
Natural source: Common Name: SARS coronavirus Taxonomy ID: 227859 Superkingdom: not available Kingdom: Viruses Genus/species: not available Coronavirus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
nsp3(527-651): GSHMGTVSWNLREMLAHAEE
TRKLMPICMDVRAIMATIQR
KYKGIKIQEGIVDYGVRFFF
YTSKEPVASIITKLNSLNEP
LVTMPIGYVTHGFNLEEAAR
CMRSLKAPAVVSVSSPDAVT
TYNGYLTSS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 481 |
| 15N chemical shifts | 130 |
| 1H chemical shifts | 925 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | nsp3(527-651) | 1 |
Entities:
Entity 1, nsp3(527-651) 129 residues - Formula weight is not available
| 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 |
Samples:
sample_13C15N: nsp3(527-651), [U-99% 13C; U-98% 15N], 1.4 mM; sodium phosphate 25 mM; sodium chloride 150 mM; sodium azide 2 mM; D2O 10%
sample_conditions_1: ionic strength: 0.227 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_13C15N | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_13C15N | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_13C15N | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_13C15N | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic region | sample_13C15N | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic region | sample_13C15N | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_13C15N | isotropic | sample_conditions_1 |
| 4D APSY-HNCOCA | sample_13C15N | isotropic | sample_conditions_1 |
| 4D APSY-HACANH | sample_13C15N | isotropic | sample_conditions_1 |
| 5D APSY-CBCACONH | sample_13C15N | isotropic | sample_conditions_1 |
| 5D APSY-HACACONH | sample_13C15N | isotropic | sample_conditions_1 |
Software:
TOPSPIN v1.3, Bruker Biospin - collection, processing
CARA v1.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
CYANA v2.0, Guntert, Mumenthaler and Wuthrich - Creating Chemical Shift List, structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
- Bruker DRX 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts