Calculate structure: Difference between revisions

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'''Domain 2 of chain A Glycogen Phosphorylase''' (<scene name='Calculate_structure/Domain_2/2'>Load Structure</scene>) - If the applet is not running the signed ver. 12 of Jmol, connect with it as you did above, and then click on the above green link.<br>
'''Domain 2 of chain A Glycogen Phosphorylase''' (<scene name='Calculate_structure/Domain_2/2'>Load Structure</scene>) - If the applet is not running the signed ver. 12 of Jmol, connect with it as you did above, and then click on the above green link.<br>
After clicking on the above green link, open the console and run the script: <center>select protein; calculate structure; cartoon; color structure; calculate hbonds structure</center><br>
After clicking on the above green link, open the console and run the script: <center>select protein; calculate structure; cartoon; color structure; calculate hbonds structure</center><br>
* <scene name='Calculate_structure/Domain_2_3turns2/6'>High lite</scene>, as four residue segments, the one residue segments in the summary below. (Remember to display the hbonds by running ''calculate hbonds structure'' from the console.) Only one segment has a residue colored blue, indicating a turn, and the other residues are colored as being part of a helix, sheet or non-secondary structure (white). Improve the view by displaying these <scene name='Calculate_structure/Domain_2_3turns3/7'>segments in isolation</scene>. but three of the segments have hbonds involved in 4-turns (773-776, 774-777, 805-808) and 5-turns (772-776, 774-778), and none of the residues involved are colored blue.  
* <scene name='Calculate_structure/Domain_2_3turns2/6'>High lite</scene>, as four residue segments, the one residue T segments in the summary below. (Remember to display the hbonds by running ''calculate hbonds structure'' from the console.) Only one segment has a residue colored blue, indicating a turn, and the other residues are colored as being part of a helix or sheet. Improve the view by displaying these <scene name='Calculate_structure/Domain_2_3turns3/7'>segments in isolation</scene>. See summary below for a description of each of these T: segments.
* Reveal the nature of the <scene name='Calculate_structure/Domain_2_4turn/2'>remaining T segments</scene>. Inspecting them for hbonds (after running ''calculate hbonds structure'' from the console) reveals that all but one of these T segments are part of β-turns, and that segment (822-825) is part of a 5-turn and two 6-turns (A type of turn not described by Miner-White, et. al.). Displaying these <scene name='Calculate_structure/Domain_2_4turn2/5'>turns in isolation</scene> makes it easier to observe the hbonds. Using the residue numbers in the summary one can determine which residues make up the turns. At two places the β-turns overlap.  All but two of the segments have at least one residue colored blue (Nitrogens involved in hbonds are also colored blue for ease of identifying hbonds.).  
* Reveal the nature of the <scene name='Calculate_structure/Domain_2_4turn/2'>remaining T segments</scene>. Inspecting them for hbonds (after running ''calculate hbonds structure'' from the console) reveals that all but one of these T segments are part of β-turns, and that segment (822-825) is part of a 4-turn and two 5-turns. Displaying these <scene name='Calculate_structure/Domain_2_4turn2/5'>turns in isolation</scene> makes it easier to observe the hbonds. Using the residue numbers in the summary one can determine which residues make up the turns. At two places the β-turns overlap.  All but two of the segments have at least one residue colored blue (Nitrogens involved in hbonds are also colored blue for ease of identifying hbonds.).  
* Using the method used for myohemerytherin above, look for β-turns that have a Pro at position 3 but do not have hbonds.
* Using the method used for myohemerytherin above, look for β-turns that have a Pro at position 3 but do not have hbonds.
   
   
'''SUMMARY of T's for Domain 2 of Chain A Glycogen Phosphorylase:'''(All other segments deleted.)<br>
'''SUMMARY of T's for Domain 2 of Chain A Glycogen Phosphorylase:'''(All other segments deleted.)<br>
T : A:488_A:488 &nbsp;&nbsp;      torsional angles: -60, -15;<br>
T : A:488_A:488 &nbsp;&nbsp;      488 (colored blue) is one residue between sheet & 3<sub>10</sub>-helix<br>
T : A:495_A:495 &nbsp;&nbsp;      torsional angles: -81, -18;<br>
T : A:495_A:495 &nbsp;&nbsp;      495 at the end of α-helix<br>
T : A:525_A:526 &nbsp;&nbsp;β-turn 524-527<br>
T : A:525_A:526 &nbsp;&nbsp;β-turn 524-527<br>
T : A:594_A:595 &nbsp;&nbsp;β-turn 593-596<br>
T : A:594_A:595 &nbsp;&nbsp;β-turn 593-596<br>
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T : A:683_A:685 &nbsp;&nbsp;β-turn 682-685<br>
T : A:683_A:685 &nbsp;&nbsp;β-turn 682-685<br>
T : A:694_A:695 &nbsp;&nbsp;β-turn 693-696<br>
T : A:694_A:695 &nbsp;&nbsp;β-turn 693-696<br>
T : A:728_A:728 &nbsp;&nbsp;      torsional angles: -34, -22;<br>
T : A:728_A:728 &nbsp;&nbsp;      728 first residue of an α-helix<br>
T : A:747_A:750 &nbsp;&nbsp;β-turn 748-751<br>
T : A:747_A:750 &nbsp;&nbsp;β-turn 748-751<br>
T : A:752_A:753 &nbsp;&nbsp;β-turn 751-754<br>
T : A:752_A:753 &nbsp;&nbsp;β-turn 751-754<br>
T : A:773_A:773 &nbsp;&nbsp;      torsional angles: -77; -79;<br>
T : A:773_A:773 &nbsp;&nbsp;      773 first residue in an α-helix <br>
T : A:777_A:777 &nbsp;&nbsp;      torsional angles: -74, -65;<br>
T : A:777_A:777 &nbsp;&nbsp;      777 part of same α-helix as 773<br>
T : A:807_A:807 &nbsp;&nbsp;      torsional angles: -93, -8;<br>
T : A:807_A:807 &nbsp;&nbsp;      807 part of an α-helix<br>
T : A:822_A:825 &nbsp;&nbsp;5-turn & two 6-turn 820-826<br>
T : A:822_A:825 &nbsp;&nbsp;4-turn & two 5-turn 820-826<br>


486-490,493-497,726-730,771-775,776-779,804-809; 524-527,593-596,610-613,633-636,636-639,668-671,675-678,682-685,693-696,748-751,751-754,820-826
486-490,493-497,726-730,771-775,776-779,804-809; 524-527,593-596,610-613,633-636,636-639,668-671,675-678,682-685,693-696,748-751,751-754,820-826