Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17468
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Citation: Feuerstein, Sophie; Solyom, Zsofia; Alada, Amine; Hoffmann, Silke; Willbold, Dieter; Brutscher, Bernhard. "1H, 13C, and 15N resonance assignment of a 179 residue fragment of hepatitis C virus non-structural protein 5A." Biomol. NMR Assignments 5, 241-243 (2011).
PubMed: 21516467
Assembly members:
NS5A_fragment_(191-369), polymer, 188 residues, 20400 Da.
Natural source: Common Name: Hepatitis C virus subtype 1b Taxonomy ID: 31647 Superkingdom: virus Kingdom: not available Genus/species: Hepacivirus Hepatitis C virus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-6P-2
Entity Sequences (FASTA):
NS5A_fragment_(191-369): GPLGSLRGGEPEPDVTVLTS
MLTDPSHITAETAKRRLARG
SPPSLASSSASQLSAPSLKA
TCTTHHDSPDADLIEANLLW
RQEMGGNITRVESENKVVIL
DSFEPLHADGDEREISVAAE
ILRKSRKFPSALPIWARPDY
NPPLLESWKDPDYVPPVVHG
CPLPPTKAPPIPPPRRKRTV
VLTESNVS
Data type | Count |
13C chemical shifts | 511 |
15N chemical shifts | 160 |
1H chemical shifts | 160 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | NS5A fragment (191-369) monomer | 1 |
Entity 1, NS5A fragment (191-369) monomer 188 residues - 20400 Da.
residue 1-9 non-native linker between protease cleavage site and NS5A residues 191-369
1 | GLY | PRO | LEU | GLY | SER | LEU | ARG | GLY | GLY | GLU | ||||
2 | PRO | GLU | PRO | ASP | VAL | THR | VAL | LEU | THR | SER | ||||
3 | MET | LEU | THR | ASP | PRO | SER | HIS | ILE | THR | ALA | ||||
4 | GLU | THR | ALA | LYS | ARG | ARG | LEU | ALA | ARG | GLY | ||||
5 | SER | PRO | PRO | SER | LEU | ALA | SER | SER | SER | ALA | ||||
6 | SER | GLN | LEU | SER | ALA | PRO | SER | LEU | LYS | ALA | ||||
7 | THR | CYS | THR | THR | HIS | HIS | ASP | SER | PRO | ASP | ||||
8 | ALA | ASP | LEU | ILE | GLU | ALA | ASN | LEU | LEU | TRP | ||||
9 | ARG | GLN | GLU | MET | GLY | GLY | ASN | ILE | THR | ARG | ||||
10 | VAL | GLU | SER | GLU | ASN | LYS | VAL | VAL | ILE | LEU | ||||
11 | ASP | SER | PHE | GLU | PRO | LEU | HIS | ALA | ASP | GLY | ||||
12 | ASP | GLU | ARG | GLU | ILE | SER | VAL | ALA | ALA | GLU | ||||
13 | ILE | LEU | ARG | LYS | SER | ARG | LYS | PHE | PRO | SER | ||||
14 | ALA | LEU | PRO | ILE | TRP | ALA | ARG | PRO | ASP | TYR | ||||
15 | ASN | PRO | PRO | LEU | LEU | GLU | SER | TRP | LYS | ASP | ||||
16 | PRO | ASP | TYR | VAL | PRO | PRO | VAL | VAL | HIS | GLY | ||||
17 | CYS | PRO | LEU | PRO | PRO | THR | LYS | ALA | PRO | PRO | ||||
18 | ILE | PRO | PRO | PRO | ARG | ARG | LYS | ARG | THR | VAL | ||||
19 | VAL | LEU | THR | GLU | SER | ASN | VAL | SER |
sample_1: NS5A fragment (191-369), [U-98% 13C; U-98% 15N], 130 uM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 20 mM; pH: 6.5; pressure: 1 atm; temperature: 278 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N BEST-TROSY | sample_1 | isotropic | sample_conditions_1 |
2D HADAMAC | sample_1 | isotropic | sample_conditions_1 |
3D BEST-TROSY HNCO | sample_1 | isotropic | sample_conditions_1 |
3D BEST-TROSY HNcoCA | sample_1 | isotropic | sample_conditions_1 |
3D BEST-TROSY iHNCA | sample_1 | isotropic | sample_conditions_1 |
3D BEST-TROSY HNcoCACB | sample_1 | isotropic | sample_conditions_1 |
3D BEST-TROSY iHNCACB | sample_1 | isotropic | sample_conditions_1 |
3D BEST-TROSY hNcocaNH | sample_1 | isotropic | sample_conditions_1 |
3D BEST-TROSY hnCOcaNH | sample_1 | isotropic | sample_conditions_1 |
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis
VNMRJ, Varian - collection
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
BMRB | 26549 |
DBJ | BAA01583 BAA02756 |
GB | AAC15722 AAC15723 AAC15724 AAC15725 AAC15726 |
SP | O92972 |
AlphaFold | O92972 |
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