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Hi E,<br>
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<p class="MsoNormal"><span style="font-size:13.0pt;line-height:107%">I
am not
familiar with the priorities of global biotechnology
neverthelles taking into
account benefits from protein folding and function prediction
and classification it is unclear why automatic domains
annotation is </span><span class="hps"><span
style="font-size:13.0pt;line-height:107%;mso-ansi-language:EN"
lang="EN">frighteningly</span></span><span
style="font-size:13.0pt;line-height:107%;mso-ansi-language:EN"
lang="EN"> <span class="hps">delayed</span> <span class="hps">compared</span>
<span class="hps">with
the amount of</span> <span class="hps">sequenced data.</span><o:p></o:p></span></p>
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style="font-size:13.0pt;line-height:107%;font-family:"Calibri","sans-serif";
mso-ascii-theme-font:minor-latin;mso-fareast-font-family:Calibri;mso-fareast-theme-font:
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New Roman";
mso-bidi-theme-font:minor-bidi;mso-ansi-language:PL;mso-fareast-language:EN-US;
mso-bidi-language:AR-SA">Is it realy so difficult to construct
reliable domains
positioning tool when strictly corelation between evolutionary
order and the
lack of random events is obvious ?</span><span
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line-height:107%;font-family:"Calibri","sans-serif";mso-ascii-theme-font:minor-latin;
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<div class="moz-cite-prefix">W dniu 2014-05-22 22:56, Elaine Meng
pisze:<br>
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<blockquote
cite="mid:2C7F1B41-2040-4C8C-8AF7-ABCD18781F8F@cgl.ucsf.edu"
type="cite">
<pre wrap="">Hi J,
It is difficult to say what is the quickest way without more information about what you are doing. As you may know, there are many different definitions of "domain" and different resources (database websites, web servers, publications, etc.) will say that the boundaries are in different places. How to quickly show these on the 3D structure depends on which resource you are using and what kind of information they provide. Further, I don't know if you are starting from only a structure or whether you have a sequence window already open.
I will try to answer, but it would help if you could be more specific with your future questions!
In general, you would go to the resource (SCOP website, or read the publication, etc.) and just look up the residue numbers for the start and end of the domain. Then you can use the residue numbers in the command line of Chimera, e.g.:
color red,r :15.a-133.a
(color ribbon-only of residues 15-133 in chain A red)
If the website or other resource shows the domain on the sequence rather than as residue numbers, another way is to show the sequence of your structure in Chimera (main menu: Favorites… Sequence) and then on the sequence drag a box around the desired part, which will also select the corresponding part of the structure. Then you can use the Actions menu to color the selected part, or command, e.g.: color red,r sel
If the domain is a feature annotation in UniProt, you can map that onto the sequence by using sequence-window menu item: "Info… UniProt Annotations" , then in the sequence window's Region Browser click on the row for that annotation to show it on both the sequence with colored boxes and structure (if any) with selection. Then you can use the Actions menu or command to color the selected part, as above. However, many UniProt entries don't have domain annotations.
I hope this helps,
Elaine
----------
Elaine C. Meng, Ph.D.
UCSF Computer Graphics Lab (Chimera team) and Babbitt Lab
Department of Pharmaceutical Chemistry
University of California, San Francisco
On May 22, 2014, at 9:59 AM, ce <a class="moz-txt-link-rfc2396E" href="mailto:allderann@gmail.com"><allderann@gmail.com></a> wrote:
</pre>
<blockquote type="cite">
<pre wrap="">Hi,
Could You send me instruction about domain colouring (the quickest way if possible) ?
Cheers,
J.
</pre>
</blockquote>
<pre wrap="">
</pre>
</blockquote>
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