Table 1.

Summary of the structure statistics

	gHH_44		gHEEE_02
Completeness of 1 H resonance assignments a, b
Backbone/side‐chain (%/%)	100/73		99.5/96.5
Conformationally restricting constraints c
Distance constraints
Total	244		1000
Intra‐residue (i = j)	104		182
Sequential (|i − j| = 1)	68		270
Medium range (1 < |i − j| < 5)	39		244
Long range (|i − j| ≥ 5)	33		301
Dihedral angle constraints	34		36
Disulfide bond constraints	3		9
Hydrogen bond constraints	20		–
No. of constraints per residue	19.5		25.9
No. of long range constraints per residue	1.3		7.5
Residual constraint violations c
Average no. of distance violations per structure:
0.1–0.2 Å	0		9.2
0.2–0.5 Å	0		2.8
>0.5 Å	0		0
Average no. of dihedral angle violations per structure:
1–10°	0		6.1
Model quality c
RMSD backbone atoms (Å)	0.41 ± 0.10		0.36 ± 0.06
RMSD heavy atoms (Å)	1.38 ± 0.13		0.90 ± 0.10
RMSD bond lengths (Å)	0.006		0.018
RMSD bond angles (°)	0.6		1.2
MolProbity Ramachandran statistics
Most favored regions (%)	97.6		92.3
Allowed regions (%)	2.4		7.6
Disallowed regions (%)	0.0		0.2
Global quality scores (Raw/Z‐score)c
Verify3D	0.41	−0.80	0.37	−1.44
ProsaII	1.31	2.73	0.95	1.24
Procheck (phi‐psi)	0.36	1.73	−0.31	−0.90
Procheck (all)d	0.02	0.12	−0.24	−1.42
MolProbity clash score	22.78	−2.38	14.40	−0.95
RPF scores
Recall/precision	0.97	0.85	0.93	0.87
F‐measure/DP‐score	0.91	0.58	0.90	0.75
BMRB accession number	30204		30312
PDB ID	5TX8		5W9F

^a  Structural statistics computed for the ensemble of 20 deposited conformers.

^b  Computed using the expected number of resonances, excluding: highly exchangeable protons (N‐terminal, Lys, and Arg amino groups, hydroxyls of Ser, Thr, Tyr).

^c  Calculated using PSVS 1.5 and based on ordered residue ranges defined by PSVS.

Ordered residues: gHH_44: C4‐N14, D17‐E24. gHEEE_02: E3‐R32, Y38‐L40.