9MEF | pdb_00009mef

Conformational flexibility in HLA-B8: peptide tuning structural and dynamical changes


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.27 Å
  • R-Value Free: 
    0.227 (Depositor), 0.237 (DCC) 
  • R-Value Work: 
    0.197 (Depositor), 0.206 (DCC) 
  • R-Value Observed: 
    0.198 (Depositor) 

Starting Model: in silico
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wwPDB Validation   3D Report Full Report


This is version 1.0 of the entry. See complete history


Literature

Conformational flexibility in HLA-B8: peptide tuning structural and dynamical changes

Li, L.Peng, X.Vinjamuri, S.Bouvier, M.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
MHC class I protein275Homo sapiensMutation(s): 1 
Gene Names: HLA-B
UniProt
Find proteins for A0A3G6II09 (Homo sapiens)
Explore A0A3G6II09 
Go to UniProtKB:  A0A3G6II09
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A3G6II09
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Beta-2-microglobulin100Homo sapiensMutation(s): 0 
Gene Names: B2MCDABP0092HDCMA22P
UniProt & NIH Common Fund Data Resources
Find proteins for P61769 (Homo sapiens)
Explore P61769 
Go to UniProtKB:  P61769
PHAROS:  P61769
GTEx:  ENSG00000166710 
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UniProt GroupP61769
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  • Reference Sequence

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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
ARG-ALA-ARG-ALA-ARG-ALA-ARG-ALA-ARG-ALA-ARG-ALA-PHE-PRO-LYS-LYS-LYS-TYR-CYS-LEU20Human immunodeficiency virus 1Mutation(s): 0 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.27 Å
  • R-Value Free:  0.227 (Depositor), 0.237 (DCC) 
  • R-Value Work:  0.197 (Depositor), 0.206 (DCC) 
  • R-Value Observed: 0.198 (Depositor) 
Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 50.75α = 90
b = 81.304β = 90
c = 110.504γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
PHASERphasing
XDSdata scaling

Structure Validation

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Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)United StatesR01 AI114467

Revision History  (Full details and data files)

  • Version 1.0: 2025-12-10
    Type: Initial release