BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16000

Title: Solution structure of the nucleocapsid-binding domain of the measles virus phosphoprotein   PubMed: 20058326

Deposition date: 2008-10-23 Original release date: 2010-05-06

Authors: Gely, Stephane; Bourhis, Jean Marie; Longhi, Sonia; Darbon, Herve; Bernard, Cedric

Citation: Gely, Stephane; Lowry, David; Bernard, Cedric; Jensen, Malene; Blackledge, Martin; Costanzo, Stephanie; Bourhis, Jean-Marie; Darbon, Herve; Daughdrill, Gary; Longhi, Sonia. "Solution structure of the C-terminal X domain of the measles virus phosphoprotein and interaction with the intrinsically disordered C-terminal domain of the nucleoprotein."  J. Mol. Recognit. 23, 435-447 (2010).

Assembly members:
XD_domain, polymer, 44 residues, 5169.205 Da.

Natural source:   Common Name: Measles   Taxonomy ID: 11234   Superkingdom: virus   Kingdom: not available   Genus/species: Morbillivirus not available

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
XD_domain: SVIRSIIKSSRLEEDRKRYL MTLLDDIKGANDLAKFHQML VKII

Data sets:
Data typeCount
1H chemical shifts289

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1XD_domain1

Entities:

Entity 1, XD_domain 44 residues - 5169.205 Da.

1   SERVALILEARGSERILEILELYSSERSER
2   ARGLEUGLUGLUASPARGLYSARGTYRLEU
3   METTHRLEULEUASPASPILELYSGLYALA
4   ASNASPLEUALALYSPHEHISGLNMETLEU
5   VALLYSILEILE

Samples:

sample_1: XD domain 1.5 uM; H2O 90%; D2O 10%

sample_2: XD domain 1.06 uM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

ARIA v1.2, Linge, O, . - chemical shift assignment, refinement, structure solution

NMR spectrometers:

  • Bruker DRX 500 MHz

Related Database Links:

BMRB 15993 15994
PDB
DBJ BAA09955 BAA09962 BAA33868 BAA33874 BAA34978
EMBL CAA34578 CAA34585 CAA91364 CAQ15998 CAQ15999
GB AAA46434 AAA46435 AAA46437 AAA63284 AAA63285
REF NP_056919
SP P03422 P35974 Q9WMB4