Table 1 NMR and refinement statistics for protein structures

From: Structural basis for the regulation of plant transcription factor WRKY33 by the VQ protein SIB1

 

SIB1-WRKY33_C

NMR distance and dihedral constraints

Distance constraints

19

   Total PRE

17

   D357C spin-labeled

8

   K376C spin-labeled

9

   Mutagenesis-derived distance restraintsa

2

   Short-range (<10 Å)

0

   Medium-range (10–20 Å)

4

   Long-range (>20 Å)

15

   Hydrogen bonds

0

Total dihedral angle restraints

0

   ϕ

-

   ψ

-

Structure statistics

 

Correlation (mean and s.d.)

   Number of conformers

20

   Between experimental data and calculated data

0.85 ± 0.01

Average pairwise r.m.s. deviation** (Å)

   Cα only

1.83 ± 0.81

   Backbone

1.86 ± 0.80

Ramachandran statistics (only for SIB1 subunit)

   Residues in most favored regions

77.8%

   Residues in additional allowed regions

20.7%

   Residues in generously allowed regions

0.3%

   Residues in disallowed regions

1.2%

  1. **Pairwise r.m.s. deviation was calculated among 20 refined structures. Only the structures of the SIB1 subunit were involved in the calculation of pairwise r.m.s. deviation.
  2. a The mutagenesis-derived distance restraints between WRKY33 I358/I360 and SIB1 V51 are set as 12.5 ± 0.5 Å
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