2K3A

NMR solution structure of Staphylococcus saprophyticus CHAP (cysteine, histidine-dependent amidohydrolases/peptidases) domain protein. Northeast Structural Genomics Consortium target SyR11

Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: target function 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history. 


Literature

Structural elucidation of the Cys-His-Glu-Asn proteolytic relay in the secreted CHAP domain enzyme from the human pathogen Staphylococcus saprophyticus.

Rossi, P., Aramini, J.M., Xiao, R., Chen, C.X., Nwosu, C., Owens, L.A., Maglaqui, M., Nair, R., Fischer, M., Acton, T.B., Honig, B., Rost, B., Montelione, G.T.

(2008) Proteins 74: 515-519


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CHAP domain protein155Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 = NCTC 7292Mutation(s): 0 
Gene Names: SSP0609
UniProt
Find proteins for Q49ZM2 (Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41))
Explore Q49ZM2 
Go to UniProtKB:  Q49ZM2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ49ZM2
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 20 
  • Selection Criteria: target function 

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: 2008-05-13
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2022-03-16
    Changes: Data collection, Database references, Derived calculations