On Tuesday, September 14, 2021 at 10:20:51 AM UTC-5 Edward K. Ream wrote:

The supplementary .pdf is *not* easy reading. Probably one needs multiple 
> PhD's to understand it.
>

Here are the supplementary videos that we mortals can enjoy.

Supplementary Video 1 
<https://static-content.springer.com/esm/art%3A10.1038%2Fs41586-021-03819-2/MediaObjects/41586_2021_3819_MOESM3_ESM.mp4>

Video of the intermediate structure trajectory of the CASP14 target T1024 
(LmrP) A two-domain target (408 residues). Both domains are folded early, 
while their packing is adjusted for a longer time.
Supplementary Video 2 
<https://static-content.springer.com/esm/art%3A10.1038%2Fs41586-021-03819-2/MediaObjects/41586_2021_3819_MOESM4_ESM.mp4>

Video of the intermediate structure trajectory of the CASP14 target T1044 
(RNA polymerase of crAss-like phage). A large protein (2180 residues), with 
multiple domains. Some domains are folded quickly, while others take a 
considerable amount of time to fold.
Supplementary Video 3 
<https://static-content.springer.com/esm/art%3A10.1038%2Fs41586-021-03819-2/MediaObjects/41586_2021_3819_MOESM5_ESM.mp4>

Video of the intermediate structure trajectory of the CASP14 target T1064 
(Orf8). A very difficult single-domain target (106 residues) that takes the 
entire depth of the network to fold.
Supplementary Video 4 
<https://static-content.springer.com/esm/art%3A10.1038%2Fs41586-021-03819-2/MediaObjects/41586_2021_3819_MOESM6_ESM.mp4>

Video of the intermediate structure trajectory of the CASP14 target 
T1091. A multi-domain target (863 residues). Individual domains’ structure 
is determined early, while the domain packing evolves throughout the 
network. The network is exploring unphysical configurations throughout the 
process, resulting in long ‘strings’ in the visualization.

Edward

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