The sequences are designed via a two-step approach. First, a novel transformer-based cross-attention GNN is employed and trained in multiple datasets. The architecture enables explicit drug-target interactions due to wiring of ligand and protein representations. The related manuscript is currently under review. During inference, we map the atom-residue interactions and identify high-attention binding pockets learned by the model. We use the identified residues to design complexes that could bind strongly to these specific residues. Three complementary strategies are applied: (i) attention-gradient following to trace high-attention paths, (ii) attention-weighted mutations that preferentially alter low-attention residues while preserving high-attention positions, and (iii) randomized sampling of high-attention regions to enhance diversity. Each candidate is evaluated with a composite score combining attention quality and consistency per residue. Structural proxies (ipSAE and iPTM), alongside an estimated ΔG and a confidence metric are also used.
id: amber-heron-pine

Nipah Virus Glycoprotein G
0.00
51.55
--
6.4 kDa
51
id: soft-shark-clay

Nipah Virus Glycoprotein G
0.00
44.90
--
6.1 kDa
51
id: ivory-goat-sand

Nipah Virus Glycoprotein G
0.27
66.40
--
6.1 kDa
51
id: gentle-moth-lotus

Nipah Virus Glycoprotein G
0.41
48.67
--
6.5 kDa
51
id: swift-seal-reed

Nipah Virus Glycoprotein G
0.00
51.21
--
6.1 kDa
51
id: noble-jaguar-ash

Nipah Virus Glycoprotein G
0.46
36.79
--
6.4 kDa
51
id: soft-fox-ruby

Nipah Virus Glycoprotein G
0.64
49.12
--
6.4 kDa
52
id: mellow-otter-leaf

Nipah Virus Glycoprotein G
0.80
47.24
--
6.2 kDa
51
id: green-mole-clay

Nipah Virus Glycoprotein G
0.10
41.09
--
6.5 kDa
51
id: pale-vole-vine

Nipah Virus Glycoprotein G
0.51
33.57
--
6.7 kDa
52