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Update pages/2_About.py

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  1. pages/2_About.py +3 -3
pages/2_About.py CHANGED
@@ -44,7 +44,7 @@ text = 'In ASCARIS representations, dimensions 1-5 correspond to datapoint ident
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  st.markdown(f'<p class="title-text">{text}</p>', unsafe_allow_html=True)
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- st.markdown('| Order of dimension | Column name in the output file | Description | Source |
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  | ------------- | ------------- | ------------- | ------------- |
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  | 1 | prot_uniprotAcc | UniProt accession | Metadata obtained from UniProtKB/Swiss-Prot |
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  | 2 | wt_residue | Wild type residue | Data obtained from UniProtKB/Swiss-Prot (humsavar), ClinVar, PMD |
@@ -56,11 +56,11 @@ st.markdown('| Order of dimension | Column name in the output file | Descriptio
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  | 8 | volume | Change in volume values upon variation. | Literature |
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  | 9 | granthamScore | Change in Grantham scores (the combination of composition, polarity and volume) values upon variation. | Literature |
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  | 10 | domains_all | InterPro Domain IDs of all domains found in the dataset | Data obtained from InterPro |
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- | 11 | domains_sig | InterPro Domain IDs of significant domains in the dataset. Domains that are not found to be significant in Fishers Exact Test are labelled as "NULL". | Data obtained from InterPro |
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  | 12 | domains_3Ddist | Shortest Euclidian distance between the domain and the variation site. | A newly engineered feature (data obtained from PDB/AlphaFold and InterPro) |
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  | 13 | sasa | Solvent accessible surface area values. | FreeSASA |
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  | 14 | location_3state | Caterozied location of the variation in the structure: surface, core or interface. | FreeSASA, InteractomeInsider |
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  | 15-44 |disulfide_bin, intMet_bin,intramembrane_bin, naturalVariant_bin, dnaBinding_bin, activeSite_bin, nucleotideBinding_bin, lipidation_bin, site_bin, transmembrane_bin, crosslink_bin, mutagenesis_bin, strand_bin, helix_bin, turn_bin, metalBinding_bin, repeat_bin, caBinding_bin, topologicalDomain_bin, bindingSite_bin, region_bin, signalPeptide_bin, modifiedResidue_bin, zincFinger_bin, motif_bin, coiledCoil_bin, peptide_bin, transitPeptide_bin, glycosylation_bin, propeptide_bin | Positional sequence annotations, binary correspondence-based (30 different types of annotations, each one on a different dimension). Categories: 0: annotatation does not exist on the protein, 1: annotation is presented, but the variation is not on the annotated site, 2: variation is on the annotated site. | Newly engineered features (data obtained from UniProtKB) |
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  | 45-74 |disulfide_dist, intMet_dist, intramembrane_dist, naturalVariant_dist, dnaBinding_dist, activeSite_dist, nucleotideBinding_dist, lipidation_dist, site_dist, transmembrane_dist, crosslink_dist, mutagenesis_dist, strand_dist, helix_dist, turn_dist, metalBinding_dist, repeat_dist, caBinding_dist, topologicalDomain_dist, bindingSite_dist, region_dist, signalPeptide_dist, modifiedResidue_dist, zincFinger_dist, motif_dist, coiledCoil_dist, peptide_dist, transitPeptide_dist, glycosylation_dist, propeptide_dist | Positional sequence annotations, distance-based (the spatial distance between the annotated residue and the mutated residue, in the protein structure, for 30 different types of annotations, each one on a different dimension), in terms of Angstroms. | Newly engineered features (data obtained from PDB/AlphaFold and UniProtKB) |
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- ')
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  st.markdown(f'<p class="title-text">{text}</p>', unsafe_allow_html=True)
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+ st.markdown("""| Order of dimension | Column name in the output file | Description | Source |
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  | ------------- | ------------- | ------------- | ------------- |
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  | 1 | prot_uniprotAcc | UniProt accession | Metadata obtained from UniProtKB/Swiss-Prot |
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  | 2 | wt_residue | Wild type residue | Data obtained from UniProtKB/Swiss-Prot (humsavar), ClinVar, PMD |
 
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  | 8 | volume | Change in volume values upon variation. | Literature |
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  | 9 | granthamScore | Change in Grantham scores (the combination of composition, polarity and volume) values upon variation. | Literature |
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  | 10 | domains_all | InterPro Domain IDs of all domains found in the dataset | Data obtained from InterPro |
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+ | 11 | domains_sig | InterPro Domain IDs of significant domains in the dataset. Domains that are not found to be significant in Fisher's Exact Test are labelled as "NULL". | Data obtained from InterPro |
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  | 12 | domains_3Ddist | Shortest Euclidian distance between the domain and the variation site. | A newly engineered feature (data obtained from PDB/AlphaFold and InterPro) |
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  | 13 | sasa | Solvent accessible surface area values. | FreeSASA |
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  | 14 | location_3state | Caterozied location of the variation in the structure: surface, core or interface. | FreeSASA, InteractomeInsider |
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  | 15-44 |disulfide_bin, intMet_bin,intramembrane_bin, naturalVariant_bin, dnaBinding_bin, activeSite_bin, nucleotideBinding_bin, lipidation_bin, site_bin, transmembrane_bin, crosslink_bin, mutagenesis_bin, strand_bin, helix_bin, turn_bin, metalBinding_bin, repeat_bin, caBinding_bin, topologicalDomain_bin, bindingSite_bin, region_bin, signalPeptide_bin, modifiedResidue_bin, zincFinger_bin, motif_bin, coiledCoil_bin, peptide_bin, transitPeptide_bin, glycosylation_bin, propeptide_bin | Positional sequence annotations, binary correspondence-based (30 different types of annotations, each one on a different dimension). Categories: 0: annotatation does not exist on the protein, 1: annotation is presented, but the variation is not on the annotated site, 2: variation is on the annotated site. | Newly engineered features (data obtained from UniProtKB) |
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  | 45-74 |disulfide_dist, intMet_dist, intramembrane_dist, naturalVariant_dist, dnaBinding_dist, activeSite_dist, nucleotideBinding_dist, lipidation_dist, site_dist, transmembrane_dist, crosslink_dist, mutagenesis_dist, strand_dist, helix_dist, turn_dist, metalBinding_dist, repeat_dist, caBinding_dist, topologicalDomain_dist, bindingSite_dist, region_dist, signalPeptide_dist, modifiedResidue_dist, zincFinger_dist, motif_dist, coiledCoil_dist, peptide_dist, transitPeptide_dist, glycosylation_dist, propeptide_dist | Positional sequence annotations, distance-based (the spatial distance between the annotated residue and the mutated residue, in the protein structure, for 30 different types of annotations, each one on a different dimension), in terms of Angstroms. | Newly engineered features (data obtained from PDB/AlphaFold and UniProtKB) |
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+ """)
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