A 2p=n , and Ak and Bk are constants. Equation 3 means

A 2p=n , and Ak and Bk are constants. Equation 3 means that each normal mode of the Cn group can be viewed as a stationary wave formed by superimposition of two waves propagating around the ring in opposite directions. The individual mode of T’ has a wave number 2p {1?n with 2 {1?wave p nodes on the ring. Schematic pictures of the T’p modes are illustrated in HDAC-IN-3 biological activity figure 3.Influence of Symmetry on Protein DynamicsMD SimulationsThe all-atom MD simulations were 64849-39-4 web performed by using IBM BlueGene/L and the RIKEN Integrated Cluster of Clusters (RICC) facility. The completely symmetric structure obtained from the normal mode analysis was used as the initial structure for each TRAP. First, the structure was solvated in TIP3P water models [42] by using Solvate plugin of VMD [43] with at least 15 ?A padding in each direction from the protein. We constructed a ?periodic box of 1116111664 A3 (73,729 atoms) for the 11-mer ?and 1136113665 A3 (77,958 atoms) for the 12-mer. Then, the solvent molecules and the hydrogen atoms in the protein were relaxed by a 2,000 step minimization with the backbone atoms restrained at the initial structure. After the relaxation, the system was gradually heated up from 0 K to 328 K (close to the growth temperature of B. stearothermophilus) in 250 ps MD simulation under the NVT ensemble. After the heating process, 100 ps simulation was performed under the NPT ensemble at 1 atm. In this stage, the backbone restraints were gradually weakened to zero. Then, the system was equilibrated in 500 1662274 ps simulation without any restraints at 328 K and 1 atm. Finally, a 100 ns production run was conducted. All the simulations were performed twice with different initial velocity conditions for each TRAP to yield two sets of 100 ns MD trajectories for each TRAP. They were qualitatively the same. All the results presented here were for one of the two. The simulations were performed using NAMD [44] with the CHARMM22 force field [38] and the CMAP corrections [39]. The particle-mesh Ewald method [45] was used to treat long?range electrostatic interactions with a direct-space cutoff of 12 A. For temperature and pressure controls, the Langevin thermostat and barostat were used [46,47].variance are classified according to their corresponding irreducible representations T’ . As shown in the figure, the T’ {T’ modes p 2 6 have similar contributions in the 11-mer and 12-mer TRAPs. The subspace spanned by the T’ and T’ modes have a half number of 1 7 degrees of freedom compared with the other modes, and thus have a half scale of the other subspaces. (TIF)Figure S2 Correlation between the normal modes and the principal modes. Correlation matrices between the normal modes and the principal modes are shown for (A) 11-mer TRAP and (B) 12-mer TRAP, respectively. (TIF) Table S1 RMS value of correlation function. Ck a? RMS values of correlation function of the Ca atom displacements by the normal modes and the principal modes are shown for 11mer and 12-mer TRAPs. (PDF)AcknowledgmentsThe authors would like to thank Hidemi Araki, Kei Moritsugu, Tadaomi Furuta, Takashi Imai, Tohru Terada, Ryuhei Harada, Hiroshi Teramoto, Mikito Toda, and Tamiki Komatsuzaki for helpful comments. The calculations were performed by using the RIKEN Integrated Cluster of Clusters (RICC) facility.Author ContributionsConceived and designed the experiments: YM RK MO JRHT AK. Performed the experiments: YM RK. Analyzed the data: YM RK. Wrote the paper: YM RK MO JRHT AK.Supporting Informatio.A 2p=n , and Ak and Bk are constants. Equation 3 means that each normal mode of the Cn group can be viewed as a stationary wave formed by superimposition of two waves propagating around the ring in opposite directions. The individual mode of T’ has a wave number 2p {1?n with 2 {1?wave p nodes on the ring. Schematic pictures of the T’p modes are illustrated in Figure 3.Influence of Symmetry on Protein DynamicsMD SimulationsThe all-atom MD simulations were performed by using IBM BlueGene/L and the RIKEN Integrated Cluster of Clusters (RICC) facility. The completely symmetric structure obtained from the normal mode analysis was used as the initial structure for each TRAP. First, the structure was solvated in TIP3P water models [42] by using Solvate plugin of VMD [43] with at least 15 ?A padding in each direction from the protein. We constructed a ?periodic box of 1116111664 A3 (73,729 atoms) for the 11-mer ?and 1136113665 A3 (77,958 atoms) for the 12-mer. Then, the solvent molecules and the hydrogen atoms in the protein were relaxed by a 2,000 step minimization with the backbone atoms restrained at the initial structure. After the relaxation, the system was gradually heated up from 0 K to 328 K (close to the growth temperature of B. stearothermophilus) in 250 ps MD simulation under the NVT ensemble. After the heating process, 100 ps simulation was performed under the NPT ensemble at 1 atm. In this stage, the backbone restraints were gradually weakened to zero. Then, the system was equilibrated in 500 1662274 ps simulation without any restraints at 328 K and 1 atm. Finally, a 100 ns production run was conducted. All the simulations were performed twice with different initial velocity conditions for each TRAP to yield two sets of 100 ns MD trajectories for each TRAP. They were qualitatively the same. All the results presented here were for one of the two. The simulations were performed using NAMD [44] with the CHARMM22 force field [38] and the CMAP corrections [39]. The particle-mesh Ewald method [45] was used to treat long?range electrostatic interactions with a direct-space cutoff of 12 A. For temperature and pressure controls, the Langevin thermostat and barostat were used [46,47].variance are classified according to their corresponding irreducible representations T’ . As shown in the figure, the T’ {T’ modes p 2 6 have similar contributions in the 11-mer and 12-mer TRAPs. The subspace spanned by the T’ and T’ modes have a half number of 1 7 degrees of freedom compared with the other modes, and thus have a half scale of the other subspaces. (TIF)Figure S2 Correlation between the normal modes and the principal modes. Correlation matrices between the normal modes and the principal modes are shown for (A) 11-mer TRAP and (B) 12-mer TRAP, respectively. (TIF) Table S1 RMS value of correlation function. Ck a? RMS values of correlation function of the Ca atom displacements by the normal modes and the principal modes are shown for 11mer and 12-mer TRAPs. (PDF)AcknowledgmentsThe authors would like to thank Hidemi Araki, Kei Moritsugu, Tadaomi Furuta, Takashi Imai, Tohru Terada, Ryuhei Harada, Hiroshi Teramoto, Mikito Toda, and Tamiki Komatsuzaki for helpful comments. The calculations were performed by using the RIKEN Integrated Cluster of Clusters (RICC) facility.Author ContributionsConceived and designed the experiments: YM RK MO JRHT AK. Performed the experiments: YM RK. Analyzed the data: YM RK. Wrote the paper: YM RK MO JRHT AK.Supporting Informatio.