Table 1. Structural statistics for the solution structure of Int^N-DNA complex.

The notation for the NMR structures is as follows: <SA> is the final 20 simulated annealing structures; $(\stackrel{‒}{\mathrm{SA}}{)}_{\mathrm{r}}$ is the average energy minimized structure. The number of terms for each restraint is given in parentheses.

	<SA>	$(\stackrel{‒}{\mathrm{SA}}{)}_{\mathrm{r}}$
R.m.s. deviations from NOE restraints (Å) a
All protein ( 664 )
sequential [ | i - j| = 1] (171)	0.041 ± 0.002	0.062
medium range [ | i - j | ≤4] (213)	0.052 ± 0.002	0.082
long range [ | i - j | ≥5 ] (132)	0.034 ± 0.005	0.047
intra-residue (148)	0.028 ± 0.008	0.062
DNA (320)
sequential (109)	0.039 ± 0.006	0.034
intraresidue (211)	0.109 ± 0.001	0.108
protein/DNA (39)	0.133 ± 0.007	0.111
R.m.s. deviations from hydrogen bonding restraints (Å) b (22)	0.056 ± 0.007	0.042
R.m.s. deviations from dihedral angles restraints (°)c (120)	0.669± 0.098	0.367
R.m.s. deviations from 3JHNα coupling constants (Hz) (20)	0.598 ± 0.041	0.761
Deviation from idealized covalent geometry
bonds (Å)	0.003 ± 0.00005	0.004
angles (°)	0.755 ± 0.003	0.817
impropers (°)	0.402 ± 0.007	0.483
PROCHECK results (%) d
most favorable region	85.9 ± 1.4	89.4
additionally allowed region	14.1 ± 1.4	10.6
generously allowed region	0.0 ± 0.0	0.0
disallowed region	0.0 ± 0.0	0.0
Coordinate Precision (Å) e
Protein backbone	0.60 ± 0.11	0.43
Protein heavy atoms	1.07 ± 0.10	0.61
All heavy atoms	0.88 ± 0.09	0.55

^aNone of the structures exhibited distance violations greater than 0.5 Å, dihedral angle violations greater than 5°, or coupling constant violations greater than 2 Hz.

^bTwo distance restraints were employed for each hydrogen bond (r_NH⋯O < 2.3 Å and r_N⋯O < 3.3 Å).

^cThe experimental dihedral angle restraints were as follows: 53 φ, 53 ψ, 11 χ₁, and 4 χ₂ angular restraints

^dDetermined using the program PROCHECK described in Ref. 46

^eThe coordinate precision is defined as the average atomic root mean square deviation (rmsd) of the 20 individual SA structures and their mean coordinates. These values are for residues Met1 to Leu64 of Int^N. The protein backbone is defined as the N, C^α, and C’ atoms.