4LMT

Structure of The N-terminal domain of Coronavirus Nucleocapsid Protein complexed with NSC663284

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.71 Å
  • R-Value Free: 0.279 
  • R-Value Work: 0.236 
  • R-Value Observed: 0.240 

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Ligand Structure Quality Assessment 


This is version 1.1 of the entry. See complete history. 


Literature

Domain of Coronavirus Nucleocapsid Protein complexed with NSC663284

Lin, S.Y., Liu, C.L., Hou, M.H.

To be published.

Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Nucleoprotein136Human coronavirus OC43Mutation(s): 0 
Gene Names: N
UniProt
Find proteins for P33469 (Human coronavirus OC43)
Explore P33469 
Go to UniProtKB:  P33469
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP33469
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
CQD
Query on CQD
Download Ideal Coordinates CCD File 
B [auth A]6-chloro-7-{[2-(morpholin-4-yl)ethyl]amino}quinoline-5,8-dione
C15 H16 Cl N3 O3
BMKPVDQDJQWBPD-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.71 Å
  • R-Value Free: 0.279 
  • R-Value Work: 0.236 
  • R-Value Observed: 0.240 
  • Space Group: P 65
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 81.911α = 90
b = 81.911β = 90
c = 42.873γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement

Structure Validation

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Ligand Structure Quality Assessment 


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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-07-16
    Type: Initial release
  • Version 1.1: 2023-11-08
    Changes: Data collection, Database references, Derived calculations, Refinement description