TABLE 1.

Summary of structure statistics

Structural statistics for the 20 NMR structures of FBP21 tandem WW domains. None of the structure exhibits distance violations >0.5 Å or dihedral angle violations >5°.

NMR restraints in the structure calculation
Distance restraints	1404
Intra-residue	392
Sequential (|i − j| = 1)	404
Medium range (|i − j| < 5)	172
Long range (|i − j| ≥ 5)	436
Dihedral angle restraints	56
Total	1460
Statistics for the 20 lowest energy structures
Lennard-Jones potential energy (kcal mol−1)	−239.15 ± 11.07
Mean r.m.s.d. from idealized covalent geometry
Bonds	0.0008 ± 0.00003 Å
Angles	0.2780 ± 0.0020°
Impropers	0.1004 ± 0.0080°
Mean r.m.s.d. from experimental restraints
Distance	0.0018 ± 0.0005 Å
cdih	0.2980 ± 0.0590°
Coordinate r.m.s.d. of N, Cα, C′/all heavy atoms (Å)a
Residues 6–32 (WW1)	0.29/0.78
Residues 47–73 (WW2)	0.35/0.86
Ramachandran plot (% residues)b
Residues in most favored regions	89.9
Residues in additional allowed regions	10
Residues in generously allowed regions	0
Residues in disallowed regions	0.1

^a The calculation of an overall r.m.s.d. is meaningless because the flexible linker caused interdomain motion.

^b Data exclude glycine, proline, and flexible residues 1–5, 13–14, 33–46, 54–55, and 74–75.