The 8 to 16 residue amino terminal linker and residues E62 to V64 of VP4 are disordered and are not ...The 8 to 16 residue amino terminal linker and residues E62 to V64 of VP4 are disordered and are not included in the model.
Remark 13
Alternate conformations are modeled for residues Q70, M82, I106, S118, T124, Q125, I141, V143, ...Alternate conformations are modeled for residues Q70, M82, I106, S118, T124, Q125, I141, V143, S151, Y155, G156, P157, Q159, K163, V167, N171, N178, E180, K187, E212, S214, and N222.
Remark 14
The G156-P157 peptide bond has alternate cis and trans conformations.
Remark 15
The model contains two apparent close contacts: the N222 side chain with HOH 2187 and the G156 ...The model contains two apparent close contacts: the N222 side chain with HOH 2187 and the G156 carbonyl with HOH 2190. In each case, the residue has alternate conformations, and the water molecule has partial occupancy, so that clashes are avoided.
Remark 16
The electron density for the K187 side chain is ambiguous beyond CB. A well-defined volume of high ...The electron density for the K187 side chain is ambiguous beyond CB. A well-defined volume of high electron density near K187 is modeled with NZ of K187 conformation B. The low B-factor of this atom (2.63) indicates that, in another conformation, this density is occupied by another atom, possibly an ion, which has not been modeled.