3BID

Crystal structure of the NMB1088 protein from Neisseria meningitidis. Northeast Structural Genomics Consortium target MR91


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.290 
  • R-Value Work: 0.241 
  • R-Value Observed: 0.241 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Crystal structure of the NMB1088 protein from Neisseria meningitidis.

Forouhar, F.Neely, H.Seetharaman, J.Mao, L.Fang, Y.Xiao, R.Owen, L.A.Maglaqui, M.Cunningham, K.Baran, M.C.Acton, T.B.Montelione, G.T.Tong, L.Hunt, J.F.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
UPF0339 protein NMB1088
A, B, C, D, E
A, B, C, D, E, F, G, H
64Neisseria meningitidis MC58Mutation(s): 0 
Gene Names: NMB1088903505
UniProt
Find proteins for Q7DDI1 (Neisseria meningitidis serogroup B (strain MC58))
Explore Q7DDI1 
Go to UniProtKB:  Q7DDI1
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ7DDI1
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A, B, C, D, E
A, B, C, D, E, F, G, H
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.290 
  • R-Value Work: 0.241 
  • R-Value Observed: 0.241 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 34.743α = 89.39
b = 60.04β = 90.81
c = 64.37γ = 103.97
Software Package:
Software NamePurpose
CNSrefinement
MAR345data collection
DENZOdata reduction
SCALEPACKdata scaling
SHELXSphasing

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2007-12-18
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2017-10-25
    Changes: Refinement description
  • Version 1.3: 2020-01-22
    Changes: Database references, Derived calculations