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Table 2 The percentages of the favored (Φ,Ψ) dihedral angles of 32 NMR protein structures before and after idealization

From: Protein Structure Idealization: How accurately is it possible to model protein structures with dihedral angles?

PDB Native Ideal Diff PDB Native Ideal Diff
1SSK 44.6% 71.9% 27.3% 2LBN 59.7% 77.6% 17.9%
2KQP 62.9% 80.0% 17.1% 1WPI 64.4% 81.4% 17.0%
1EXE 60.5% 76.7% 16.2% 2LNV 58.6% 72.4% 13.8%
1X6F 64.1% 73.1% 9.0% 2L6B 72.2% 81.1% 8.9%
2GFU 72.3% 80.4% 8.1% 1PC2 79.3% 87.4% 8.1%
2LMR 79.7% 87.0% 7.3% 2KA0 72.6% 78.3% 5.7%
2L3O 71.3% 76.9% 5.6% 1O1W 67.2% 72.1% 4.9%
2CQ9 78.3% 82.6% 4.3% 2RQA 72.0% 75.4% 3.4%
2D86 89.0% 92.1% 3.1% 1NTC 80.5% 83.1% 2.6%
2JZT 76.6% 79.0% 2.4% 2CZN 76.5% 76.5% 0.0%
1RCH 75.4% 74.6% -0.8% 2JU1 77.1% 75.9% -1.2%
2KV7 85.5% 84.2% -1.3% 2JT2 83.6% 81.5% -2.1%
2KYW 83.8% 81.1% -2.7% 2OSR 82.7% 80.0% -2.7%
2L6M 81.7% 78.5% -3.2% 2CU1 81.1% 77.8% -3.3%
1AJ3 93.3% 88.8% -4.5% 1WI5 84.0% 78.0% -6.0%
1NMW 85.0% 78.0% -7.0% 2LBV 83.9% 74.8% -9.1%