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The RNA binding interface is also extremely diverse for the four Brix proteins.
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Water molecules in the coenzyme binding interface are also found in many dinucleotide binding domains and may be important for specificity and modulating affinity.
In addition, we provide evidence that suggests that resonances from tryptophans distant from the binding interface are also stabilized by the receptor.
Interestingly, 2 residues shown through crystallography to be contacts in the binding interface were also identified as being under diversifying selection (D48 and I115 in CPXV-BR, E48 and L115 in ECTV).
Communication between DNA-binding lobes and the dimer interface is also reflected in the modest stabilization of both domains D1 and D2 on DNA binding (Table 1).
A VWIC interface is also required.
The user interface is also simplified with only 3 buttons.
Its search interface is also available on handhelds.
The structure of μ3 subunit of AP-3 complex was also solved with TGN38 sorting signal peptide, and the binding interface is similar to that on μ2-TGN38 [ 48].
We also present evidence that the eIF2Bβ/δ binding interface is similar to that in the eIF2Bα2 homodimer.
The Norrin Fz4CRD binding interface is conserved between the complex structures.
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