And if I might suggest; for efficiency reasons it would make sense to share and read and think about these questions beforehand. Maybe even type some answers and just paste them. That leaves more time for us to read and respond to your answers.
Hi there!
We do understand the need for more feedback, and we've been working diligently over time to help improve the quality and speed of the communication back from the team, however we do appreciate this feedback and will take it to heart as we know it's an ongoing process for improvement.
(Keep in mind though with certain things like collaborations/publications, they are often dependent on partners/outside factors we are working with - no excuses, just the reality we all have to work with.)
R plots, like ED, seem to be most useful when used with crystallography. For us non- scientists, can you help us understand when these tools are more useful than other modes of studying a protein.
Could we possibly have the view of ideal loops in cartoon mode? most of us work in that mode rather than stick mode and we might produce better results
Y'all gave us the basic information for the Rama map, but can we know how we should or could apply it and how to use it? Y'all also gave us the possible native states for the loops, but how would we replicate them? We're also able to click on a plot and drag it around. What's the purpose of this? It seems like it's another way to pull the protein. Is there a preference between plots being scattered and plots being clustered?
Lastly, I just noticed the other day in selection interface that, to loops, we can press 5. Is there a difference between using idealize (2) and pressing 5? (I can't remember the name of the function for 5)
Thanks!