|Entry||Database: PDB / ID: 5lxj|
|Title||Solution NMR structure of the X domain of Peste des Petits Ruminants phosphoprotein|
|Keywords||VIRAL PROTEIN / XD domain Nucleocapsid binding domain / STRUCTURE FROM CYANA 3.97|
|Function / homology|
Function and homology information
viral genome replication / viral nucleocapsid / RNA-directed 5'-3' RNA polymerase activity / transcription, DNA-templated / RNA binding
Similarity search - Function
RNA polymerase, phosphoprotein P, C-terminal XD, paramyxovirinae / Paramyxovirus structural protein P/V, N-terminal domain / Paramyxovirus structural protein V/P N-terminus / P/V phosphoprotein, paramyxoviral / Paramyxovirus P/V phosphoprotein C-terminal / Ubiquitin-associated (UBA) domain / Helicase, Ruva Protein; domain 3 / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Similarity search - Component
|Biological species||Peste-des-petits-ruminants virus|
|Method||SOLUTION NMR / torsion angle dynamics|
|Authors||Pereira, N. / Piuzzi, M. / Bontems, F. / Eleouet, J.-F. / Sizun, C.|
|Citation||Journal: To Be Published|
Title: Solution structure of the X domain of Peste des Petits Ruminants Virus phosphoprotein and interaction with the nucleoprotein
Authors: Pereira, N. / Basbous, N. / Piuzzi, M. / Bontems, F. / Eleouet, J.-F. / Sizun, C.
|Structure viewer||Molecule: |
Downloads & links
|#1: Protein|| |
Mass: 5964.977 Da / Num. of mol.: 1 / Fragment: X domain, UNP residues 459-509
Source method: isolated from a genetically manipulated source
Details: This peptide contains residues S459-P509. The two N-terminal GS residues are left from an N-terminal GST-tag cleaved with thrombin.
Source: (gene. exp.) Peste-des-petits-ruminants virus / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q91QS4
|Experiment||Method: SOLUTION NMR|
|Sample conditions||Ionic strength: 300 mM / Ionic strength err: 30 / Label: 288K / pH: 7.4 / Pressure: 1 bar / Temperature: 288.0 K / Temperature err: 0.2|
|Refinement||Method: torsion angle dynamics / Software ordinal: 5|
|NMR representative||Selection criteria: target function|
|NMR ensemble||Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20|
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