>example-D1 (66 residues) FVAELNNLLGREVQVVLSNGEVYKGVLHAVDNQLNIVLANASNKAGEKFNRVFIYRYIVH IDSTER |
Sequence |
20 40 60 | | | FVAELNNLLGREVQVVLSNGEVYKGVLHAVDNQLNIVLANASNKAGEKFNRVFIYRYIVHIDSTER |
Prediction | CHHHHHHHCCCSSSSSSCCCCSSSSSSSSSCCCCSSSSSSCSCCCCCSCCSSSSSSSSSSSSSCCC |
Conf.Score | 957888765988999986996999999996787479997533568985557999888888753469 |
H:Helix; S:Strand; C:Coil | |
Sequence |
20 40 60 | | | FVAELNNLLGREVQVVLSNGEVYKGVLHAVDNQLNIVLANASNKAGEKFNRVFIYRYIVHIDSTER |
Prediction | 744414522444040304636414020212345023102313466454232010331133044268 |
Values range from 0 (buried residue) to 8 (highly exposed residue) | |
|
LOMETS threading is guided by the consensus contact map (left figure) and distance map (right figure) derived based on confidence scores of DeepPotential. In the contact and distance maps, the axes mark the residue index along the sequence. For the contact map, each dot represents a residue pair with predicted contact, while for the distance map a color scale represents a distance of 1-20+ angstroms. No dot is close to the diagonal in the contact map, because LOMETS does not consider contacts for residue pairs separated by <4 residues. |
Rank | PDB Hit | RCSB Link | CMO | MAE | ID1 | ID2 | Cov | Norm. Zscore | Download Alignment | 20 40 60 | | | | |||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Sec.Str. Sol.Acc. Seq | CHHHHHHHCCCSSSSSSCCCCSSSSSSSSSCCCCSSSSSSCSCCCCCSCCSSSSSSSSSSSSSCCC 744414522444040304636414020212345023102313466454232010331133044268 FVAELNNLLGREVQVVLSNGEVYKGVLHAVDNQLNIVLANASNKAGEKFNRVFIYRYIVHIDSTER | ||||||||||||||||||||||||||||||||||||
1 | 4c8qE | 4c8q | 0.805 | 1.194 | 0.17 | 0.17 | 1.00 | 1.19 | HHpred | PLEVIDKTINQKVLIVLQSNREFEGTLVGFDDFVNVILEDAVEWVMQHHGRMLLSNNIAILVPGGK | |||||||||||||||||||||||||||
2 | 5mkiA | 5mki | 0.846 | 1.087 | 0.24 | 0.23 | 0.95 | 2.22 | SparksX | PLDALGKSINTNVTVYLKDGKLVKGRLKAYDLHMNVALENAKIESEKEFPMLVVRDNVLYVSL--- | |||||||||||||||||||||||||||
3 | 4c8qE | 4c8q | 0.805 | 1.194 | 0.17 | 0.17 | 1.00 | 1.27 | HHsearch | PLEVIDKTINQKVLIVLQSNREFEGTLVGFDDFVNVILEDAVEWVMQHHGRMLLSNNIAILVPGGK | |||||||||||||||||||||||||||
4 | 5nrll | 5nrl | 0.893 | 1.099 | 0.24 | 0.24 | 1.00 | 1.38 | MUSTER | LVNFLKKLRNEQVTIELKNGTTVWGTLQSVSPQMNAILTDVKLTLPASLQYINIRNTIRQIILPDS | |||||||||||||||||||||||||||
5 | 5mqfe | 5mqf | 0.765 | 1.491 | 0.20 | 0.20 | 0.98 | 1.07 | FFAS3D | -IKVLHEAEGHIVTCETNTGEVYRGKLIEAEDNMNCQMSNITVTYRDQLEQVYIRGSKIRFLILPD | |||||||||||||||||||||||||||
6 | 5ganr | 5gan | 0.758 | 1.203 | 0.18 | 0.18 | 1.00 | 1.33 | HHpred | STPELKKYMDKKILLNINGSRKVAGILRGYDIFLNVVLDDAMEINNHQLGQTVIRNSIISLEALDA | |||||||||||||||||||||||||||
7 | 3swnA | 3swn | 0.866 | 1.169 | 0.17 | 0.17 | 1.00 | 2.17 | SparksX | PLELIDKCIGSNLWVIMKSEREFAGTLVGFDDYVNIVLKDVTEYDTEKHSEMLLNGGMCMLIPGGK | |||||||||||||||||||||||||||
8 | 3jb9G | 3jb9 | 0.805 | 1.060 | 0.17 | 0.17 | 1.00 | 1.27 | HHsearch | PLSVLQQAVHDQVLINCRNNKKLLARVKAFDRHSNMVLENVKEMKDRFISKMFLRDGVVLVVRIPS | |||||||||||||||||||||||||||
9 | 5mqfg | 5mqf | 0.852 | 1.104 | 0.21 | 0.21 | 1.00 | 1.28 | MUSTER | LVRFLMKLSHETVTIELKNGTQVHGTITGVDVSMNTHLKAVKMTLKVQLETLSIRNNIRYFILPDS | |||||||||||||||||||||||||||
10 | 5nrll | 5nrl | 0.832 | 1.456 | 0.21 | 0.21 | 1.00 | 1.05 | FFAS3D | LVNFLKKLRNEQVTIELKNGTTVWGTLQSVSPQMNAILTDVKLTLPNSLQYINIRGNTIRQIILPD | |||||||||||||||||||||||||||
| |||||||||||||||||||||||||||||||||||||
|
Download Model 1 |
Download Model 2 |
Download Model 3 |
Download Model 4 |
Download Model 5 |
Top 10 structural analogues in PDB (as identified by
TM-align)
|
Function and Ligand Binding Annotation for Proteins with Similar Structure |
(a) | PDB Hit is the PDB of the specific domain/chain aligned to Model 1 |
(b) | RCSB Link is the RCSB PDB link of the full-length protein. |
(c) | Gene Ontology (GO) term and Enzyme Commission (EC) number list the function annotations for structurally aligned proteins, as collected by BioLiP database. |
(d) | Ligand lists known binding ligands for each aligned protein, as collected by BioLiP database. |
(e) | Binding Site Residues lists the known binding residues for each ligand as collected by BioLiP database. The residue numbering is based on the specfic domain/chain numbering and highlighted residues means they are present in the alignment with Model 1.
Note: Listed binding residues may not be representative of the full ligand binding pocket and may be part of a complex with another protein chain/domain. Also, for a single ligand, one template may have multiple binding sites. |
(a) | Templates are ranked in descending order of normalized Z-score, as explained by (i) below. |
(b) | PDB Hit is the PDB of the specific domain/chain aligned to the query. |
(c) | RCSB Link is the RCSB PDB link of the full-length protein. |
(d) | CMO is the contact map overlap score, calculated from the number of overlapping contacts between the predicted contact map and the contact map derived from the aligned template, then normalized by the number of predicted contacts. |
(e) | MAE is the mean absolute error between the predicted distance map and the distance map derived from the aligned template. |
(f) | ID1 is the number of template residues identical to query divided by the number of aligned residues. |
(g) | ID2 is the number of template residues identical to query divided by the query sequence length. |
(h) | Cov is equal to the number of aligned template residues divided by the query sequence length. |
(i) | Norm. Zscore is the normalized Z-score of the threading alignments. A normalized Z-score ≥1 means a good alignment. |
(j) | Download PDB provides the structure of the aligned region for each template. |
(k) | Download FASTA provides the fasta format and full-length alignment of model and template. Shows alignment for potential ligand binding pockets and GO/EC terms. |
(l) | Gene Ontology (GO) term and Enzyme Commission (EC) number list the function annotations for template proteins, as collected by BioLiP database. |
(m) | Ligand lists known binding ligands for each template protein, as collected by BioLiP database. |
(n) | Binding Site Residues lists the known binding residues for each ligand as collected by BioLiP database. The residue numbering is based on the template PDB numbering and highlighted residues means they are aligned with the query sequence.
Note: Listed binding residues may not be representative of the full ligand binding pocket and may be part of a complex with another protein chain/domain. Also, for a single ligand, one template may have multiple binding sites. |
Templates from Hybrid-CEthreader |
Templates from SparksX |
Templates from CEthreader |
Templates from HHsearch |
Templates from MapAlign |
Templates from MUSTER |
Templates from MRFsearch |
Templates from DisCovER |
Templates from FFAS3D |
Templates from EigenThreader |
Templates from HHpred |
References: | |
1. | W Zheng, Q Wuyun, X Zhou, Y Li, P Freddolino, Y Zhang. LOMETS3: Integrating deep-learning and profile-alignment for advanced protein template recognition and function annotation. in preparation, (2021) |
2. | W Zheng, C Zhang, Q Wuyun, R Pearce, Y Li, Y Zhang. LOMETS2: improved meta-threading server for fold-recognition and structure-based function annotation for distant-homology proteins. Nucleic Acids Research, 47: W429-W436 (2019). |
3. | S Wu, Y Zhang. LOMETS: A local meta-threading-server for protein structure prediction. Nucleic Acids Research, 35: 3375-3382 (2007). |