Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25809
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Citation: Camilloni, Carlo; Sala, Benedetta Maria; Sormanni, Pietro; Porcari, Riccardo; Corazza, Alessandra; De Rosa, Matteo; Zanini, Stefano; Barbiroli, Alberto; Esposito, Gennaro; Bolognesi, Martino; Bellotti, Vittorio; Vendruscolo, Michele; Ricagno, Stefano. "Rational design of mutations that change the aggregation rate of a protein while maintaining its native structure and stability" Sci. Rep. 6, 25559-25559 (2016).
PubMed: 27150430
Assembly members:
W60G_b2m, polymer, 100 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: PHN1
Entity Sequences (FASTA):
W60G_b2m: MIQRTPKIQVYSRHPAENGK
SNFLNCYVSGFHPSDIEVDL
LKNGERIEKVEHSDLSFSKD
GSFYLLYYTEFTPTEKDEYA
CRVNHVTLSQPKIVKWDRDM
Data type | Count |
13C chemical shifts | 375 |
15N chemical shifts | 99 |
1H chemical shifts | 497 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | W60G_beta2-microglobulin | 1 |
Entity 1, W60G_beta2-microglobulin 100 residues - Formula weight is not available
1 | MET | ILE | GLN | ARG | THR | PRO | LYS | ILE | GLN | VAL | |
2 | TYR | SER | ARG | HIS | PRO | ALA | GLU | ASN | GLY | LYS | |
3 | SER | ASN | PHE | LEU | ASN | CYS | TYR | VAL | SER | GLY | |
4 | PHE | HIS | PRO | SER | ASP | ILE | GLU | VAL | ASP | LEU | |
5 | LEU | LYS | ASN | GLY | GLU | ARG | ILE | GLU | LYS | VAL | |
6 | GLU | HIS | SER | ASP | LEU | SER | PHE | SER | LYS | ASP | |
7 | GLY | SER | PHE | TYR | LEU | LEU | TYR | TYR | THR | GLU | |
8 | PHE | THR | PRO | THR | GLU | LYS | ASP | GLU | TYR | ALA | |
9 | CYS | ARG | VAL | ASN | HIS | VAL | THR | LEU | SER | GLN | |
10 | PRO | LYS | ILE | VAL | LYS | TRP | ASP | ARG | ASP | MET |
sample_1: W60G_b2m, [U-98% 13C; U-98% 15N], 0.7 mM; D2O, [U-99% 2H], 5%; sodium phosphate 70 mM; sodium chloride 100 mM; H2O 95%
sample_conditions_1: ionic strength: 0.19 M; pH: 6.6; pressure: 1 atm; temperature: 310 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D H(C)CH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
SPARKY, Goddard - chemical shift assignment
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks