BMRB Entry 4101
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4101
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Citation: Prompers, Jeanine; Groenewegen, Anneke; van_Schaik, Rene; Pepermans, Henri; Hilbers, Cornelis. "1H, 13C, and 15N Resonance Assignments of Fusarium Solani Pisi Cutinase
and Preliminary Features of the Structure in Solution" Protein Sci. 6, 2374-2384 (1997).
Assembly members:
Fusarium solani pisi cutinase, polymer, 214 residues, 22212 Da.
Natural source: Common Name: fungus Taxonomy ID: 29915 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Fusarium solani
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: CT1
Entity Sequences (FASTA):
Fusarium solani pisi cutinase: APTSNPAQELEARQLGRTTR
DDLINGNSASCADVIFIYAR
GSTETGNLGTLGPSIASNLE
SAFGKDGVWIQGVGGAYRAT
LGDNALPRGTSSAAIREMLG
LFQQANTKCPDATLIAGGYS
QGAALAAASIEDLDSAIRDK
IAGTVLFGYTKNLQNRGRIP
NYPADRTKVFCNTGDLVCTG
SLIVAAPHLAYGPDARGPAP
EFLIEKVRAVRGSA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 905 |
| 15N chemical shifts | 230 |
| 1H chemical shifts | 1368 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | cutinase | 1 |
Entities:
Entity 1, cutinase 214 residues - 22212 Da.
| 1 | ALA | PRO | THR | SER | ASN | PRO | ALA | GLN | GLU | LEU | ||||
| 2 | GLU | ALA | ARG | GLN | LEU | GLY | ARG | THR | THR | ARG | ||||
| 3 | ASP | ASP | LEU | ILE | ASN | GLY | ASN | SER | ALA | SER | ||||
| 4 | CYS | ALA | ASP | VAL | ILE | PHE | ILE | TYR | ALA | ARG | ||||
| 5 | GLY | SER | THR | GLU | THR | GLY | ASN | LEU | GLY | THR | ||||
| 6 | LEU | GLY | PRO | SER | ILE | ALA | SER | ASN | LEU | GLU | ||||
| 7 | SER | ALA | PHE | GLY | LYS | ASP | GLY | VAL | TRP | ILE | ||||
| 8 | GLN | GLY | VAL | GLY | GLY | ALA | TYR | ARG | ALA | THR | ||||
| 9 | LEU | GLY | ASP | ASN | ALA | LEU | PRO | ARG | GLY | THR | ||||
| 10 | SER | SER | ALA | ALA | ILE | ARG | GLU | MET | LEU | GLY | ||||
| 11 | LEU | PHE | GLN | GLN | ALA | ASN | THR | LYS | CYS | PRO | ||||
| 12 | ASP | ALA | THR | LEU | ILE | ALA | GLY | GLY | TYR | SER | ||||
| 13 | GLN | GLY | ALA | ALA | LEU | ALA | ALA | ALA | SER | ILE | ||||
| 14 | GLU | ASP | LEU | ASP | SER | ALA | ILE | ARG | ASP | LYS | ||||
| 15 | ILE | ALA | GLY | THR | VAL | LEU | PHE | GLY | TYR | THR | ||||
| 16 | LYS | ASN | LEU | GLN | ASN | ARG | GLY | ARG | ILE | PRO | ||||
| 17 | ASN | TYR | PRO | ALA | ASP | ARG | THR | LYS | VAL | PHE | ||||
| 18 | CYS | ASN | THR | GLY | ASP | LEU | VAL | CYS | THR | GLY | ||||
| 19 | SER | LEU | ILE | VAL | ALA | ALA | PRO | HIS | LEU | ALA | ||||
| 20 | TYR | GLY | PRO | ASP | ALA | ARG | GLY | PRO | ALA | PRO | ||||
| 21 | GLU | PHE | LEU | ILE | GLU | LYS | VAL | ARG | ALA | VAL | ||||
| 22 | ARG | GLY | SER | ALA |
Related Database Links:
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