Sentence examples for backbone atoms from the from inspiring English sources

The time-series of the root-mean-square-deviation (RMSD) of backbone atoms from the initial PDB structures is shown in Figure 2.

Root-mean-square deviations (RMSD) of the backbone atoms from the different protein structures were computed from the MD trajectory relative to the initial structures to estimate the stabilization of the systems (Supporting Figures S8 and S9).

The resulting structure deviated by less than 0.3 Å (rms value for all N, Cα, CO backbone atoms) from the structure shown in Figure 2. To v): For both KTX solution) and KTX solid), structure calculations were performed without and with restraints for the three disulphide bonds.

The resulting structure deviated by less than 0.7 Å (rms value for all N, Cα, CO backbone atoms) from the structure shown in Figure 2. To iv): Peak intensities obtained from the 2D CHHC and NHHC spectra were classified into four ranges and converted into distance ranges of 1.8 2.7, 1.8 3.3, 1.8 5.0 and 1.8 6.0 Å, respectively.

Nevertheless, when using these three CHHC spectra together with the 2D NHHC spectrum, the resulting structure deviated by less than 0.7 Å (rms value for all N, Cα, CO backbone atoms) from the structure shown in Figure 2. To ii): At the end of pass 1 and 2 the PASD algorithm calculates likelihood estimates that each particular assignment associated with a cross-peak is correct.

With the indirubin-bound structure, the backbone atoms from the loop move up to 8 Å closer to the active site.

Although there are many different methods to represent an RNA conformation, this simplified representation enables us to rapidly rebuild backbone atoms from angles.

Data are shown as the root mean square deviations for the backbone atoms (N CA C O) from the experimental structure, over 10 ns for the four tetrameric combinations depicted in Table 1.

Structural drift of the helix was measured by calculating the mean root-mean-square deviation (rmsd) of the backbone Cα atoms from the starting structure over the last 25 ns of each simulation.

To explore the dynamic stability of the two AChE/inhibitor complexes and to ensure the rationality of the sampling strategy, the time-dependent RMSD values of the complex backbone atoms were calculated from the X-ray crystal structure of AChE during MD trajectories of 10 ns.

The first type of interactions involves the main chain backbone atoms of the β2 strands from both proteins.