3IL8

CRYSTAL STRUCTURE OF INTERLEUKIN 8: SYMBIOSIS OF NMR AND CRYSTALLOGRAPHY


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Observed: 0.187 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Crystal structure of interleukin 8: symbiosis of NMR and crystallography.

Baldwin, E.T.Weber, I.T.St Charles, R.Xuan, J.C.Appella, E.Yamada, M.Matsushima, K.Edwards, B.F.Clore, G.M.Gronenborn, A.M.Wlodawer, A.

(1991) Proc Natl Acad Sci U S A 88: 502-506

  • DOI: https://doi.org/10.1073/pnas.88.2.502
  • Primary Citation of Related Structures:  
    3IL8

  • PubMed Abstract: 

    The crystal structure of a host defense system chemotactic factor, interleukin 8, has been solved by molecular replacement using as a model the solution structure derived from nuclear magnetic resonance experiments. The structure was refined with 2 A x-ray data to an R factor of 0.187 (0.217 at 1.6 A). A comparison indicates some potential differences between the structure in solution and in the crystalline state. Our analysis also predicts that residues 4 through 9 on the amino terminus and the beta-bend, which includes His-33, may be important for receptor binding.


  • Organizational Affiliation

    Crystallography Laboratory, National Cancer Institute-Frederick Cancer Research and Development Center, MD 21702.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
INTERLEUKIN-872Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P10145 (Homo sapiens)
Explore P10145 
Go to UniProtKB:  P10145
PHAROS:  P10145
GTEx:  ENSG00000169429 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP10145
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Observed: 0.187 
  • Space Group: P 31 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 40.3α = 90
b = 40.3β = 90
c = 90.1γ = 120
Software Package:
Software NamePurpose
PROLSQrefinement

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 1992-10-15
    Type: Initial release
  • Version 1.1: 2008-03-25
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2012-02-29
    Changes: Database references