Table 1. NMR and refinement statistics... | Rockefeller University Press

Table 1.

NMR and refinement statistics of the Binder/α-tubulin complex

NMR restraints
Unambiguous restraints (intermolecular NOEs)	58
Ambiguous restraints (CSPs)	10
HADDOCK parameters
Cluster Size	200
HADDOCK score	−71.7 (± 1.2)
Van Der Waals energy	−34.2 (± 3.4)
Electrostatic energy	−262.1 (± 27.8)
Restraints violation energy	+4.6 (± 0.7)
Buried surface area	+1163.3 (± 25.1)
All backbone	0.4
All heavy atoms	0.6
RMS deviations^a
Bond angles	0.6°
Bond lengths	0.004 Å
Molprobity clashscore^b	2.5 (99th percentile)
Ramachandran statistics^a
Most favored (%)	90.8
Additionally allowed (%)	9.1
Generously allowed (%)	0.1
Disallowed (%)	0.0

NMR restraints
Unambiguous restraints (intermolecular NOEs)	58
Ambiguous restraints (CSPs)	10
HADDOCK parameters
Cluster Size	200
HADDOCK score	−71.7 (± 1.2)
Van Der Waals energy	−34.2 (± 3.4)
Electrostatic energy	−262.1 (± 27.8)
Restraints violation energy	+4.6 (± 0.7)
Buried surface area	+1163.3 (± 25.1)
All backbone	0.4
All heavy atoms	0.6
RMS deviations^a
Bond angles	0.6°
Bond lengths	0.004 Å
Molprobity clashscore^b	2.5 (99th percentile)
Ramachandran statistics^a
Most favored (%)	90.8
Additionally allowed (%)	9.1
Generously allowed (%)	0.1
Disallowed (%)	0.0

Calculated for an ensemble of 20 lowest energy structures.

Calculated for the lowest energy structure.