BMRB Entry 17451
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17451
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Title: Central domain of RSV M2-1 PubMed: 21523439
Deposition date: 2011-02-09 Original release date: 2011-05-03
Authors: Dubosclard, Virginie; Blondot, Marie-Lise; Eleouet, Jean-Francois; Bontems, Francois; Sizun, Christina
Citation: Dubosclard, Virginie; Blondot, Marie-Lise; Eleouet, Jean-Francois; Bontems, Francois; Sizun, Christina. "1H, 13C, and 15N resonance assignment of the central domain of hRSV transcription antitermination factor M2-1." Biomol. NMR Assignments 5, 237-239 (2011).
Assembly members:
M2-1, polymer, 121 residues, Formula weight is not available
Natural source: Common Name: Human syncytial respiratory virus Taxonomy ID: 11245 Superkingdom: virus Kingdom: not available Genus/species: Pneumovirus Human respiratory syncytial virus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
M2-1: GSEISGAAELDRTEEYALGV
VGVLESYIGSINNITKQSAC
VAMSKLLTELNSDDIKKLRD
NEEPNSPKIRVYNTVISYIE
SNRKNNKQTIHLLKRLPADV
LKKTIKNTLDIHKSITINNP
K
- assigned_chemical_shifts
- RDCs
Data type | Count |
13C chemical shifts | 533 |
15N chemical shifts | 129 |
1H chemical shifts | 889 |
residual dipolar couplings | 100 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | M2-1 | 1 |
Entities:
Entity 1, M2-1 121 residues - Formula weight is not available
The two first residues GS are left after cleavage of the N-terminal GST tag. The M2-1 sequence starts at Glu59 and ends with Lys177.
1 | GLY | SER | GLU | ILE | SER | GLY | ALA | ALA | GLU | LEU | ||||
2 | ASP | ARG | THR | GLU | GLU | TYR | ALA | LEU | GLY | VAL | ||||
3 | VAL | GLY | VAL | LEU | GLU | SER | TYR | ILE | GLY | SER | ||||
4 | ILE | ASN | ASN | ILE | THR | LYS | GLN | SER | ALA | CYS | ||||
5 | VAL | ALA | MET | SER | LYS | LEU | LEU | THR | GLU | LEU | ||||
6 | ASN | SER | ASP | ASP | ILE | LYS | LYS | LEU | ARG | ASP | ||||
7 | ASN | GLU | GLU | PRO | ASN | SER | PRO | LYS | ILE | ARG | ||||
8 | VAL | TYR | ASN | THR | VAL | ILE | SER | TYR | ILE | GLU | ||||
9 | SER | ASN | ARG | LYS | ASN | ASN | LYS | GLN | THR | ILE | ||||
10 | HIS | LEU | LEU | LYS | ARG | LEU | PRO | ALA | ASP | VAL | ||||
11 | LEU | LYS | LYS | THR | ILE | LYS | ASN | THR | LEU | ASP | ||||
12 | ILE | HIS | LYS | SER | ILE | THR | ILE | ASN | ASN | PRO | ||||
13 | LYS |
Samples:
M21-15N13C: M2-1, [U-100% 13C; U-100% 15N], 0.13 mM; sodium phosphate 50 mM; sodium chloride 150 mM; DTT 1 mM; H2O 93%; D2O 7%
M21-13C: M2-1, [U-100% 13C], 0.1 mM; sodium phosphate 50 mM; sodium chloride 150 mM; DTT 1 mM; D2O 100%
M21-15N-c12e5: M2-1, [U-100% 15N], 0.2 mM; sodium phosphate 50 mM; sodium chloride 150 mM; DTT 1 mM; c12e5 0.055 v/v; Hexanol 0.017 v/v; H2O 93%; D2O 7%
M21-15N-gel: M2-1, [U-100% 15N], 0.12 mM; sodium phosphate 50 mM; sodium chloride 150 mM; DTT 1 mM; acrylamide/bisacryamide 6%; H2O 93%; D2O 7%
M21-15N: M2-1, [U-100% 15N], 0.12 mM; sodium phosphate 50 mM; sodium chloride 150 mM; DTT 1 mM; H2O 93%; D2O 7%
sample_conditions_1: ionic strength: 150 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | M21-15N13C | isotropic | sample_conditions_1 |
3D HNCO | M21-15N13C | isotropic | sample_conditions_1 |
3D HNCA | M21-15N13C | isotropic | sample_conditions_1 |
3D HN(CO)CA | M21-15N13C | isotropic | sample_conditions_1 |
3D HNCACB | M21-15N13C | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | M21-15N13C | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | M21-15N | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | M21-13C | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | M21-13C | isotropic | sample_conditions_1 |
3D HCCH-TOCSY aromatic | M21-13C | isotropic | sample_conditions_1 |
3D CCH-TOCSY | M21-13C | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | M21-13C | isotropic | sample_conditions_1 |
2D HBCBCGCDHD | M21-13C | isotropic | sample_conditions_1 |
2D 1H-15N IPAP HSQC | M21-15N-c12e5 | anisotropic | sample_conditions_1 |
2D 1H-15N IPAP HSQC | M21-15N-gel | anisotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - collection, processing
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - data analysis, peak picking
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
- Bruker Avance 950 MHz
Related Database Links:
PDB | |
DBJ | BAA00106 |
GB | AAB59860 AAB86665 AAB86677 AAC14903 AAC55971 |
REF | NP_044597 |
SP | P04545 |
Download simulated HSQC data in one of the following formats:
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SPARKY: Backbone
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