2nla protein structure has 26 interfacial amino acids within 5.0 Å cut-off distance. After the interfacial mutation scanning step, 494 possible mutations were built. As the result of box-whisker statistics, 34 outliers were detected within a 2.5xIQR whisker threshold. Among them 0 most enriching and 34 most Depleting Mutations are proposed as designer mutations.

The most Depleting Mutation is G262W with 82.68 ΔΔG score.

The residue that is most frequently leading to a binding depleting is G262.

The residue that is most frequently leading to a binding enriching is V321.

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Final List of Proposed Designer Mutations
Position Mutation ΔΔG Protein Stability Score Mutation Impact on Protein Folding ΔΔG Binding Affinity Score Mutation Impact on Protein Binding
V220 Y 0.4 Negative 5.72 Negative
V253 F -0.24 Positive 4.78 Negative
V253 W -0.64 Positive 6.72 Negative
V253 Y -0.07 Positive 6.5 Negative
D256 P 1.7 Negative 5.29 Negative
G262 A -0.25 Positive 4.75 Negative
G262 C 0.17 Negative 10.34 Negative
G262 D -0.49 Positive 19.06 Negative
G262 E -1.46 Positive 19.24 Negative
G262 F -1.57 Positive 42.56 Negative
G262 H -0.26 Positive 29.86 Negative
G262 I -1.34 Positive 29.84 Negative
G262 K -0.96 Positive 29.44 Negative
G262 L -1.31 Positive 31.27 Negative
G262 M -1.04 Positive 20.47 Negative
G262 N -0.27 Positive 19.36 Negative
G262 P -2.69 Positive 11.71 Negative
G262 Q -0.48 Positive 21.32 Negative
G262 R -0.7 Positive 28.16 Negative
G262 S -0.02 Positive 9.29 Negative
G262 T 0.1 Negative 18.31 Negative
G262 V -0.55 Positive 18.63 Negative
G262 W -1.51 Positive 82.68 Negative
G262 Y -1.64 Positive 44.16 Negative
R263 F -1.56 Positive 6.38 Negative
R263 W 0.11 Negative 9.3 Negative
R263 Y -1.29 Positive 7.54 Negative
V265 R 4.7 Negative 6.59 Negative
T266 F -1.4 Positive 13.4 Negative
T266 H -0.39 Positive 6.26 Negative
T266 K -0.74 Positive 5.5 Negative
T266 R -0.39 Positive 6.72 Negative
T266 W -1.94 Positive 19.16 Negative
T266 Y -1.43 Positive 15.03 Negative