Structural basis for broad detection of genogroup II noroviruses by a monoclonal antibody that binds to a site occluded in the viral particle

> Summary

Summary for 3V7A

Descriptor5B18 heavy chain, 5B18 kappa chain, Capsid (3 entities in total)
Functional Keywordsvirus, protein-fab complex, broadly-reactive antibody, immune system
Biological sourceHuman calicivirus
Total number of polymer chains6
Total molecular weight163978.02
Hansman, G.S.,Mclellan, J.S.,Kwong, P.D. (deposition date: 2011-12-20, release date: 2012-02-08, Last modification date: 2013-09-25)
Primary citation
Hansman, G.S.,Taylor, D.W.,McLellan, J.S.,Smith, T.J.,Georgiev, I.,Tame, J.R.,Park, S.Y.,Yamazaki, M.,Gondaira, F.,Miki, M.,Katayama, K.,Murata, K.,Kwong, P.D.
Structural Basis for Broad Detection of Genogroup II Noroviruses by a Monoclonal Antibody That Binds to a Site Occluded in the Viral Particle.
J.Virol., 86:3635-3646, 2012
PubMed: 22278249 (PDB entries with the same primary citation)
DOI: 10.1128/JVI.06868-11
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.277130.1%3.7%0.1%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

Molmil generated image of 3v7a
no rotation
Molmil generated image of 3v7a
rotated about x axis by 90°
Molmil generated image of 3v7a
rotated about y axis by 90°

> Structural details

Sequence viewer

Contents of the asymmetric unit

PolymersNumber of chains6
Total molecular weight163978.0
Non-Polymers*Number of molecules0
Total molecular weight0.0
All*Total molecular weight163978.0
*Water molecules are not included.

> Experimental details

Refinement Statistics

Experimental method:X-RAY DIFFRACTION (3.297 Å)

Cell axes145.480145.480216.334
Cell angles90.0090.0090.00
SpacegroupP 43 2 2
Resolution limits31.54 - 3.30
the highest resolution shell value3.404 - 3.297
the highest resolution shell value0.349
the highest resolution shell value0.432
RMSD bond length0.004
RMSD bond angle0.795

Data Collection Statistics

Resolution limits31.54 - 3.30
the highest resolution shell value -
Number of reflections30833

Crystallization Conditions

crystal IDmethodpHpH rangetemperatureunit

Crystallization Reagents

IDcrystal IDsolution IDreagent nameconcentrationdetails
Crystallization Reagents in Literatures*
IDcrystal IDsolutionreagent nameconcentration (unit)details
Annotated Information is extracted from Literature Info*

> Functional details


Functional Information from GO Data

A0019028cellular_componentviral capsid
B0019028cellular_componentviral capsid

Functional Information from PDB Data

site_idNumber of ResiduesDetails

Functional Information from PDB atom coordinates for the "HETATM" binding sites

site_idNumber of ResiduesDetails

Functional Information from PROSITE/UniProt

site_idNumber of ResiduesDetails

Functional Information from SwissProt/UniProt

site_idNumber of ResiduesDetails

Catalytic Information from CSA

site_idNumber of ResiduesDetails

> Sequence Neighbor

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