1665: Symmetric Dimer Design: 70 Residues

Summary

Name:

Status:

Closed

Created:

04/22/2019

Points:

100

Expired:

04/29/2019 - 23:00

Difficulty:

Intermediate

Description:

This symmetric design puzzle has C2 symmetry, with two symmetric chains. There is no H-bond Network Objective in this puzzle, so the interface can be completely nonpolar (orange sidechains). No more than 50% of residues may form helices, and all loops must match one of the Ideal Loop Building Blocks found in the Blueprint tool. See the puzzle comments for Objective details. The Baker Lab will run folding predictions on your solutions for this puzzle, and those that perform well will be synthesized in the lab. Remember, you can use the Upload for Scientists button for up to 5 designs that you want us to look at, even if they are not the best-scoring solutions!

Categories:

Design, Overall, Symmetry

Rank

Group

Score

Points

Beta Folders

20,966

100

20,883

20,748

20,720

20,366

Rank

Player

Group

Score

Points

LociOiling 4 1

Beta Folders

20,966

100

20,883

20,882

20,865

20,862

Rank

Player

Group

Score

Points

LociOiling 4 1

Beta Folders

20,964

100

20,879

20,854

20,728

20,717

Mon, 04/22/2019 - 23:23

bkoep 70 412

Offline

Joined: 11/15/2012

Groups: Foldit Staff

Objectives

Core Existence: Monomer (max +2000)
Ensures that at least 20 residues are buried in the core of the monomer unit.

Core Existence: Complex (max +2300)
Ensures that at least 46 residues are buried in the core of the entire complex (including the interface between monomer units).

SS Design (max +500)
Penalizes all CYS residues. Penalizes GLY, ALA residues in sheets. Penalizes GLY, ALA, SER, THR in helices.

Ideal Loops (max +500)
Penalizes any loop region that does not match one of the Building Blocks in the Blueprint tool. Use "Auto Structures" to see which regions of your protein count as loops.

Secondary Structure (max +500)
No more than 50% of residues may form helices. Extra helices are penalized at 10 points per residue.