Evidence: SAXS, Size-exclusion chromatography-coupled small-angle X-ray scattering (SEC-SAXS) was performed to assess the oligomerisation state of glycosylated (high mannose) Nariva virus receptor ...Evidence: SAXS, Size-exclusion chromatography-coupled small-angle X-ray scattering (SEC-SAXS) was performed to assess the oligomerisation state of glycosylated (high mannose) Nariva virus receptor binding protein in solution. Using the dimeric crystal structure data a best fitting model was generated using molecular dynamics, which considered the flexibility of the high mannose N-linked glycans and C- and N-termini. The extensive homodimeric interface observed in the crystal structure was largely retained.
Type
Name
Symmetry operation
Number
identity operation
1_555
x,y,z
1
Unit cell
Length a, b, c (Å)
55.382, 82.957, 92.988
Angle α, β, γ (deg.)
90.000, 90.860, 90.000
Int Tables number
4
Space group name H-M
P1211
Noncrystallographic symmetry (NCS)
NCS domain:
ID
Ens-ID
Details
1
1
chainA
2
1
(chainBandresid198through626)
NCS domain segments:
Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: ALA / Beg label comp-ID: ALA / End auth comp-ID: ASN / End label comp-ID: ASN / Auth seq-ID: 198 - 626 / Label seq-ID: 198 - 626
Dom-ID
Selection details
Auth asym-ID
Label asym-ID
1
chainA
A
A
2
(chainBandresid198through626)
B
B
-
Components
#1: Protein
Attachmentprotein
Mass: 72484.414 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Nariva narmovirus Cell line (production host): Human embryonic kidney 293T cells Production host: Homo sapiens (human) / References: UniProt: B8XH64
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