Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19770
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Citation: Kold, David; Dauter, Zbigniew; Laustsen, Anne; Brzozowski, Andrzej; Turkenburg, Johan; Nielsen, Anders; Koldsoe, Heidi; Petersen, Evamaria; Schioett, Birgit; De Maria, Leonardo; Wilson, Keith; Svendsen, Allan; Wimmer, Reinhard. "Thermodynamic and structural investigation of the specific SDS binding of Humicola insolens cutinase" Protein Sci. 23, 1023-1035 (2014).
PubMed: 24832484
Assembly members:
cutinase, polymer, 194 residues, Formula weight is not available
Natural source: Common Name: ascomycetes Taxonomy ID: 34413 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Humicola insolens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: N/A
Data type | Count |
13C chemical shifts | 364 |
15N chemical shifts | 156 |
1H chemical shifts | 283 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | cutinase | 1 |
Entity 1, cutinase 194 residues - Formula weight is not available
Residue GLU 1 was converted into pyroglutamate when expressing the protein in minimal media in E.coli
1 | PCA | LEU | GLY | ALA | ILE | GLU | ASN | GLY | LEU | GLU | ||||
2 | SER | GLY | SER | ALA | ASN | ALA | CYS | PRO | ASP | ALA | ||||
3 | ILE | LEU | ILE | PHE | ALA | ARG | GLY | SER | THR | GLU | ||||
4 | PRO | GLY | ASN | MET | GLY | ILE | THR | VAL | GLY | PRO | ||||
5 | ALA | LEU | ALA | ASN | GLY | LEU | GLU | SER | HIS | ILE | ||||
6 | ARG | ASN | ILE | TRP | ILE | GLN | GLY | VAL | GLY | GLY | ||||
7 | PRO | TYR | ASP | ALA | ALA | LEU | ALA | THR | ASN | PHE | ||||
8 | LEU | PRO | ARG | GLY | THR | SER | GLN | ALA | ASN | ILE | ||||
9 | ASP | GLU | GLY | LYS | ARG | LEU | PHE | ALA | LEU | ALA | ||||
10 | ASN | GLN | LYS | CYS | PRO | ASN | THR | PRO | VAL | VAL | ||||
11 | ALA | GLY | GLY | TYR | SER | GLN | GLY | ALA | ALA | LEU | ||||
12 | ILE | ALA | ALA | ALA | VAL | SER | GLU | LEU | SER | GLY | ||||
13 | ALA | VAL | LYS | GLU | GLN | VAL | LYS | GLY | VAL | ALA | ||||
14 | LEU | PHE | GLY | TYR | THR | GLN | ASN | LEU | GLN | ASN | ||||
15 | ARG | GLY | GLY | ILE | PRO | ASN | TYR | PRO | ARG | GLU | ||||
16 | ARG | THR | LYS | VAL | PHE | CYS | ASN | VAL | GLY | ASP | ||||
17 | ALA | VAL | CYS | THR | GLY | THR | LEU | ILE | ILE | THR | ||||
18 | PRO | ALA | HIS | LEU | SER | TYR | THR | ILE | GLU | ALA | ||||
19 | ARG | GLY | GLU | ALA | ALA | ARG | PHE | LEU | ARG | ASP | ||||
20 | ARG | ILE | ARG | ALA |
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