| File | Description | File size | Download |
|---|---|---|---|
| β-glucosidases info | CSV fileID; Organism; Protein name; UNIPROT ID; Lenght; |
245K | db_info.csv |
| PDB files | Modeled by homology with MODELLER | 247M | db.zip |
| Sequences | FASTA format | 1.6M | db.fasta |
| Secondary structure information (calculated by DSSP) | FASTA format>UNIPROT ID | H = α-helix
B = residue in isolated β-bridge
E = extended strand, participates in β ladder
G = 3-helix (310 helix)
I = 5 helix (π-helix)
T = hydrogen bonded turn
S = bend |
1.6M | secondary_structure.fasta |
| List of conserved residues based on multiple alignment. | CSV file | 211K | CONSERVED_RESIDUES_2.csv |
| Number of contacts between ligand and wild protein (determined by ARPEGGIO) | Tabular fileUNIPROT (Uniprot ID + mutation) HB (hydrogen bond) WHB (weak hydrogen bond) I (ionic contact) A (aromatic contact) P (polar contact) WP (weak polar contact) H (hydrophobic contact) |
1.7M | contacts_wild.tsv |
| Number of contacts between ligand and mutant proteins (determined by ARPEGGIO) | Tabular fileUNIPROT (Uniprot ID + mutation) HB (hydrogen bond) WHB (weak hydrogen bond) I (ionic contact) A (aromatic contact) P (polar contact) WP (weak polar contact) H (hydrophobic contact) |
2.8M | contacts_mutant.tsv |
| List of mutants | Text fileUniProt ID | Mutation |
78K | mutations.txt |
| Extrapoled mutations | CSV fileUniProt ID | origin residue | global residue | extrapoled mutation | ID UniProt origin |
179K | EXTRAPOLATED_MUTATIONS.csv |
Designed by:
Prof. Dr. Raquel de Melo-Minardi
Dr. Diego Mariano
Back-end:
Naiara Pantuza, M.Sc. / Dr. Diego Mariano
Front-end:
Naiara Pantuza, M.Sc. / Dr. Diego Mariano
Financing and support:
CAPES / UFMG / LBS