1OZO

Three-dimensional solution structure of apo-S100P protein determined by NMR spectroscopy

Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 50 
  • Conformers Submitted: 16 
  • Selection Criteria: structures with the least restraint violations,structures with the lowest energy 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history. 


Literature

NMR structure of the Apo-S100P protein.

Lee, Y.-C., Volk, D.E., Thiviyanathan, V., Kleerekoper, Q., Gribenko, A.V., Zhang, S., Gorenstein, D.G., Makhatadze, G.I., Luxon, B.A.

(2004) J Biomol NMR 29: 399-402


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
S-100P protein
A, B
95Homo sapiensMutation(s): 0 
Gene Names: S100P OR S100E
UniProt & NIH Common Fund Data Resources
Find proteins for P25815 (Homo sapiens)
Explore P25815 
Go to UniProtKB:  P25815
PHAROS:  P25815
GTEx:  ENSG00000163993 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP25815
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 50 
  • Conformers Submitted: 16 
  • Selection Criteria: structures with the least restraint violations,structures with the lowest energy 

Structure Validation

View Full Validation Report



View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2004-04-20
    Type: Initial release
  • Version 1.1: 2008-04-29
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-02-23
    Changes: Data collection, Database references, Derived calculations