In situ structure of nebulin bound to actin filament in skeletal sarcomere. Determined by electron microscopy at 4.5 Å resolution. Released 16 Mar 2022.
Explore 7QIM in 3D Show helices and sheets RCSB PDB PDBe
7QIM contains 117 α-helices and 105 β-strands across 7 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-11 | 4 | 15 |
| β-strand | 17-21 | 5 | 15 |
| β-strand | 22 | 1 | 16 |
| β-strand | 24 | 1 | 16 |
| β-strand | 29-31 | 3 | 15 |
| β-strand | 35-37 | 3 | 17 |
| α-helix | 48-49 | 2 | |
| β-strand | 53-54 | 2 | 17 |
| α-helix | 55-61 | 7 | |
| β-strand | 66-68 | 3 | 17 |
| β-strand | 71-72 | 2 | 18 |
| β-strand | 75-76 | 2 | 18 |
| α-helix | 79-88 | 10 | |
| α-helix | 89-94 | 6 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 15 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 15 |
| α-helix | 137-145 | 9 | |
| β-strand | 150-154 | 5 | 19 |
| β-strand | 160-162 | 3 | 20 |
| β-strand | 163-166 | 4 | 19 |
| β-strand | 169-170 | 2 | 19 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 20 |
| α-helix | 182-193 | 12 | |
| α-helix | 203-215 | 13 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 21 |
| β-strand | 247-250 | 4 | 21 |
| α-helix | 253-262 | 10 | |
| α-helix | 274-284 | 11 | |
| α-helix | 290-295 | 6 | |
| β-strand | 298-300 | 3 | 19 |
| α-helix | 301-304 | 4 | |
| α-helix | 309-320 | 12 | |
| α-helix | 335-337 | 3 | |
| α-helix | 338-348 | 11 | |
| α-helix | 351-355 | 5 | |
| β-strand | 357-358 | 2 | 15 |
| α-helix | 359-364 | 6 | |
| α-helix | 368-373 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-17 | 13 | |
| α-helix | 19-23 | 5 | |
| α-helix | 24-28 | 5 | |
| α-helix | 29-31 | 3 | |
| α-helix | 40-52 | 13 | |
| α-helix | 54-65 | 12 | |
| α-helix | 75-86 | 12 | |
| α-helix | 89-102 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-17 | 13 | |
| α-helix | 19-31 | 13 | |
| α-helix | 40-52 | 13 | |
| α-helix | 54-65 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| ACTS protein | A, B, C, D, E | protein | 377 | Mus musculus | P68134 (AlphaFold model) |
| nebulin (mouse) | F | protein | 105 | Mus musculus | |
| nebulin (mouse) | G | protein | 70 | Mus musculus |
>7QIM_1 ACTS protein (chains A, B, C, D, E) MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT KQEYDEAGPSIVHRKCF
>7QIM_2 nebulin (mouse) (chains F) XXXXXXXXXXXXXXXXXXXXXYXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXYXXX XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXYXXXXXXXXXXXXX
>7QIM_3 nebulin (mouse) (chains G) XXXXXXXXXXXXXXXXXXXXXYXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXYXXX XXXXXXXXXX
Structures from intact myofibrils reveal mechanism of thin filament regulation through nebulin. Wang, Z., Grange, M., Pospich, S. et al. Science (2022) 375:eabn1934-eabn1934. DOI 10.1126/science.abn1934 · PubMed
Other PDB entries of the same protein (UniProt P68134 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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