TABLE 1.
Bitopic proteins in Membranome 3.0 | Superposition of AF2 models with PDB structures a | ||||||
---|---|---|---|---|---|---|---|
Species | N prot b | N AF2 c | N AF2 c | Rover‐AF2 d | Rover‐AF2 e (%) | RMSD f (Å) | Identity g (%) |
H. sapiens | 2,383 | 2,368 | 788 | 271 ± 184 | 53 ± 22 | 1.5 ± 0.9 | 97 ± 10 |
A. thaliana | 2,105 | 2069 | 52 | 215 ± 106 | 51 ± 24 | 1.0 ± 1.0 | 98 ± 4 |
S. Cerevisiae | 383 | 374 | 69 | 104 ± 21 | 26 ± 17 | 1.1 ± 0.5 | 100 ± 1 |
D. discoideum | 605 | 598 | 0 | 0 | 0 | 0 | 0 |
E. coli | 205 | 204 | 34 | 476 ± 358 | 83 ± 10 | 2.8 ± 1.8 | 99 ± 1 |
M. jannaschii | 77 | 77 | 4 | 131 ± 29 | 77 ± 9 | 0.6 ± 0.5 | 99 ± 1 |
Average values with SD. One PDB entry with the largest number of overlapped residues was selected for each protein.
N prot, number of bitopic proteins.
N AF2, number of AF2 models included in Membranome database.
R over‐AF2, number of overlapping residues between AF2 model and PDB structure.
Percentage of overlapping residues between AF2 model and PDB structure.
RMSD for Cα‐atoms.
Sequence identity between overlapping residues in AF2 models and PDB structures.