1AYM

HUMAN RHINOVIRUS 16 COAT PROTEIN AT HIGH RESOLUTION


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.15 Å
  • R-Value Free: 0.233 
  • R-Value Work: 0.230 
  • R-Value Observed: 0.230 

wwPDB Validation   3D Report Full Report


This is version 2.2 of the entry. See complete history


Literature

The refined structure of human rhinovirus 16 at 2.15 A resolution: implications for the viral life cycle.

Hadfield, A.T.Lee, W.Zhao, R.Oliveira, M.A.Minor, I.Rueckert, R.R.Rossmann, M.G.

(1997) Structure 5: 427-441

  • DOI: https://doi.org/10.1016/s0969-2126(97)00199-8
  • Primary Citation of Related Structures:  
    1AYM

  • PubMed Abstract: 

    Rhinoviruses belong to the picornavirus family and are small, icosahedral, non-enveloped viruses containing one positive RNA strand. Human rhinovirus 16 (HRV16) belongs to the major receptor group of rhinoviruses, for which the cellular receptor is intercellular adhesion molecule-1 (ICAM-1). In many rhinoviruses, one of the viral coat proteins (VP1) contains a hydrophobic pocket which is occupied by a fatty acid-like molecule, or so-called 'pocket factor'. Antiviral agents have been shown to bind to the hydrophobic pocket in VP1, replacing the pocket factor. The presence of the antiviral compound blocks uncoating of the virus and in some cases inhibits receptor attachment. A refined, high-resolution structure would be expected to provide further information on the nature of the pocket factor and other features previously not clearly identified.


  • Organizational Affiliation

    Department of Biological Sciences, Purdue University West Lafayette, IN 47907-1392, USA.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
HUMAN RHINOVIRUS 16 COAT PROTEINA [auth 1]285Human rhinovirus sp.Mutation(s): 0 
UniProt
Find proteins for Q82122 (Human rhinovirus 16)
Explore Q82122 
Go to UniProtKB:  Q82122
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UniProt GroupQ82122
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
HUMAN RHINOVIRUS 16 COAT PROTEINB [auth 2]261Human rhinovirus sp.Mutation(s): 0 
UniProt
Find proteins for Q82122 (Human rhinovirus 16)
Explore Q82122 
Go to UniProtKB:  Q82122
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UniProt GroupQ82122
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
HUMAN RHINOVIRUS 16 COAT PROTEINC [auth 3]238Human rhinovirus sp.Mutation(s): 0 
UniProt
Find proteins for Q82122 (Human rhinovirus 16)
Explore Q82122 
Go to UniProtKB:  Q82122
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UniProt GroupQ82122
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  • Reference Sequence
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
HUMAN RHINOVIRUS 16 COAT PROTEIND [auth 4]68Human rhinovirus sp.Mutation(s): 0 
UniProt
Find proteins for P23008 (Human rhinovirus 1A)
Explore P23008 
Go to UniProtKB:  P23008
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UniProt GroupP23008
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.15 Å
  • R-Value Free: 0.233 
  • R-Value Work: 0.230 
  • R-Value Observed: 0.230 
  • Space Group: P 2 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 362.6α = 90
b = 347.1β = 90
c = 334.9γ = 90
Software Package:
Software NamePurpose
X-PLORmodel building
X-PLORrefinement
DENZOdata reduction
SCALEPACKdata scaling
X-PLORphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-01-21
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-07-04
    Changes: Advisory, Data collection, Derived calculations, Other
  • Version 2.0: 2023-02-08
    Type: Remediation
    Changes: Atomic model, Data collection, Database references, Derived calculations, Other, Refinement description
  • Version 2.1: 2023-03-15
    Changes: Advisory
  • Version 2.2: 2023-08-09
    Changes: Refinement description