We used parametrically designed proteins that are small, easily expressed, and very stable. We used their sequence in a custom boltz2-solubleMPNN iterative redesign cycle. We only accepted boltz2 prediction that increased in ipSAE_min for the next generation of designs. We found that changing 10% of residues to X in random positions kickstarts this process of refinement. Ultimately the fold and core of these miniproteins remains mostly unchanged while ipSAE_min could go up to 0.8. We expect high success rate in expressibility and stability of these binders. We borrowed code from ProteinHunter to run Boltz and sollubleMPNN.
id: wild-bear-maple

Nipah Virus Glycoprotein G
None
89.38
True
12.5 kDa
109
id: crimson-falcon-orchid

Nipah Virus Glycoprotein G
None
89.07
True
10.7 kDa
96
id: pale-bear-thorn

Nipah Virus Glycoprotein G
None
60.22
True
13.2 kDa
116
id: shy-bison-sand

Nipah Virus Glycoprotein G
None
86.44
True
7.0 kDa
58
id: strong-tiger-thorn

Nipah Virus Glycoprotein G
None
67.99
True
6.8 kDa
58
id: green-bear-cedar

Nipah Virus Glycoprotein G
0.78
88.39
--
10.6 kDa
86