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We report detailed numerical and spectroscopic studies of two complexes from a family of recently discovered MnIII6 single-molecule magnets (SMMs) with large barriers to magnetization reversal.
We randomly select two complexes from each cluster if it has more than one protein complex.
Guided by the structural analysis (Table 1), two complexes from the BINAP series (L7 and L8) were tested as catalysts because they have similar Au⋅⋅⋅Au distances (>5.3 Å).
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HUD took control of the four complexes from the Housing Authority of New Orleans in 2002 because of accusations of financial mismanagement.
The electron transport chain in mitochondria, which consists of five complexes from I to V, is the major site of ATP production.
Two out of six complexes from class I behaved differently.
One officer patrols the two complexes daily from 4 p.m. to midnight.
The subunits for the two complexes were from structurally unrelated SCOP Superfamilies (SCOP IDs are 47203 and 56645 for the first complex, and 81338 for both subunits of the second complex).
Here, we demonstrate that the two complexes can be prepared from the same protein components, confirming that neither complex is the product of misfolded protein samples.
Figure 9 Exemplary comparison of YASARA, Protonate 3D and Protoss predictions on two complex structures from the Astex Set (PDB codes 1t46 and 1hq2).
Thereby, the hydrogen bond to Cys87 is replaced by a contact of two donors with a hydrogen distance of 1.21 Å. Figure 8 Exemplary comparison of YASARA, Protonate 3D and Protoss predictions on two complex structures from the Astex Set (PDB codes 1n46 and 2br1).
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