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2052: IL-2R Binder Design: Round 6
Status: Closed
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Soloists
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| 51 | AlphaFold2 46 84 | AlphaFold | 10,843 | 3 | | 52 | pascal ochem 46 1603 | Go Science | 10,805 | 3 | | 53 | tracybutt 46 113 | Beta Folders | 10,667 | 2 | | 54 | Oransche 19 71 | Marvin's bunch | 10,649 | 2 | | 55 | Larini 46 45 | | 10,390 | 2 | | 56 | Alistair69 46 112 | L'Alliance Francophone | 10,368 | 2 | | 57 | Merf 46 73 | | 10,156 | 2 | | 58 | kevin ever... 46 103 | | 10,091 | 2 | | 59 | Dr.Sillem 46 27 | | 10,087 | 1 | | 60 | scottwuzhear 46 641 | | 10,069 | 1 | | 61 | rinze 46 53 | | 10,058 | 1 | | 62 | Trajan464 46 85 | | 9,944 | 1 | | 63 | BarrySampson 46 54 | | 9,809 | 1 | | 64 | ManVsYard 46 526 | Gargleblasters | 9,802 | 1 | | 65 | kentish_alex 46 641 | | 9,618 | 1 | | 66 | petetrig 46 949 | Go Science | 8,909 | 1 | | 67 | vinsi 46 1603 | | 8,613 | 1 | | 68 | Flagg65a 46 356 | | 8,332 | 1 | | 69 | deathbat_87 46 721 | | 8,326 | 1 | | 70 | SHK5P 46 554 | | 8,313 | 1 | | 71 | BogdanW3 46 1603 | | 7,601 | 1 | | 72 | rezaefar 46 122 | | 7,498 | 1 | | 73 | DScott 46 122 | | 7,467 | 1 | | 74 | fsk8r 46 1603 | | 6,954 | 1 | | 75 | zo3xiaJonWeinberg 46 96 | Team China | 6,587 | 1 | Need this puzzle? Log in to download.
Comments
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DDG Metric (max +2000)
The predicted binding energy of your design. The goal DDG is -40.0 or less.
Contact Surface (max +2000)
Measures how much of your binder surface is in close contact with the target protein. The goal Contact Surface is 500 or more.
Buried Unsats (max +500)
Penalizes 100 points for each polar atom that cannot make any hydrogen bonds.
Core Existence (max +1500)
Ensures that at least 25 percent of residues are buried in the core of the monomer unit.
Interaction Energy (max +500)
Monitors that all large PHE, TYR, and TRP residues are scoring well.
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.
SS Design (max +500)
Disabled use of CYS residues. Penalizes GLY, ALA residues in sheets and helices.