603: CASP10 Refinement Puzzle: TR705

Closed since over 13 years ago

Summary

• Created: July 22, 2012
• Expires: July 31, 2012 at 16:00 UTC
• Max points: 100

Description

This is the thirteenth CASP10 Refinement Target. This model was the best server prediction for target T0705, generated by the AOBA-server. We've been told that ~65% of this model matches the native, so you'll need to significantly change the starting model. Luckily, this is a short target with only 96 residues. Note: Cut Tool is available on this puzzle.

Top groups

• 21. DSN @ Home 1 pt. 9,111
• 22. Geekdo 1 pt. 9,108
• 23. Nerdfighters 1 pt. 9,008
• 24. null pointer exception 1 pt. 7,269
• 25. test_group1 1 pt. 6,838

Top soloists

• 91. Tyggy Too 8 pts. 9,958
• 92. phi16 8 pts. 9,955
• 93. Auntiesocial 8 pts. 9,955
• 94. jogie62 7 pts. 9,954
• 95. truestone 7 pts. 9,952
• 96. tallguy-13088 7 pts. 9,949
• 97. abiogenesis 7 pts. 9,948
• 98. c1261015 6 pts. 9,945
• 99. sjoerdouwe 6 pts. 9,944
• 100. Andi1960 6 pts. 9,943

Comments

[beta_helix]

This is the page for this CASP10 refinement target:
http://predictioncenter.org/casp10/target.cgi?id=192

Note that the organizers gave us this hint:

"Starting model GDT_TS=65."

GDT_TS=65 essentially means that ONLY 65% of the model superimposes correctly onto the native structure:

en.wikipedia.org

Global distance test

The global distance test (GDT), also written as GDT_TS to represent "total score", is a measure of similarity between two protein structures with known amino acid correspondences (e.g. identical amino acid sequences) but different tertiary structures. It is most commonly used to compare the results of protein structure prediction to the experimentally determined structure as measured by X-ray crystallography, protein NMR, or, increasingly, cryoelectron microscopy. The metric was developed by Ada...

Here is the sequence logo predicted by the SAM server:

H = helix
E = sheet
C = loop (or coil)

The taller the letter at each position, the higher the probability of that specific secondary structure for that amino acid.

For example, the Valines at residues 19, 20 & 76 are highly predicted to be part of a sheet. However, the Valine at residue 38 is predicted to be anything.