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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%