Table 6. Shape entropy in the protein condensed phase: polar cage.

The occurrence of shape entropy is determined by the fluctuation of 49 surface-exposed amino-acid residues in the crystal contacts of the transcriptional antiterminator (PDB entry 3gwh). Differences between C^α atoms and the terminal amino-acid residues are shown as a measure of surface conformational entropy. Some amino-acid side chains of residues located at the edges of the asymmetric unit switch directions, occupy neighboring cage walls within the ensemble or lose contact with the symmetry-related molecule.

Ensemble member No.	Differences in Cα atoms (Å)	Differences in terminal side-chain atoms (Å)	Occurrence of side chains in cage walls
1	0.98	1.20	−100, −1−10, 001, 00−1, −10−1, 100, 0−10, 0−1−1
2	0.90	1.81	−100, −1−10, 001, −10−1, 00−1, 100, 0−10, 0−1−1
3	0.81	1.36	−100, −1−10, 001, 00−1, −10−1, 100, 0−10, 0−1−1
4	1.03	1.50	−100, −1−10, 001, −10−1, 00−1, 100, 0−10, 0−1−1
5	0.73	1.38	−100, −1−10, 001, 00−1, −10−1, 100, 0−10, 0−1−1
6	0.75	1.25	−100, −1−10, 001, 00−1, −10−1, 100, 0−10, 0−1−1
7	0.79	1.37	−100, −1−10, 001, −10−1, 00−1, 100, 0−10, 001, 0−1−1
8	1.08	1.51	−100, −1−10, 001, −10−1, 100, 0−10, 0−1−1, 00−1
9	0.87	1.52	−100, −1−10, 001,−10−1, 00−1, 100, 0−10, 0−1−1, −10−1
10	0.84	1.76	−100, −1−10, 001, 00−1, −10−1, 100, 0−10, −10−1, 0−1−1
Minimum	0.73	1.20
Maximum	1.08	1.81