BMRB Entry 30037

Click here to enlarge.

PDB ID: 6ht4
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30037
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
NMR Structure of NS5A-D2 (JFH1) peptide (304-323)
Deposition date:
2016-03-18
Original release date:
2019-07-15
Authors:
Dujardin, M.; Cantrelle, F.; Lippens, G.; Hanoulle, X.
Citation:

Citation: Dujardin, Marie; Madan, Vanesa; Gandhi, Neha; Cantrelle, Francois-Xavier; Launay, Helene; Huvent, Isabelle; Bartenschlager, Ralf; Lippens, Guy; Hanoulle, Xavier. "Cyclophilin A allows the allosteric regulation of a structural motif in the disordered domain 2 of NS5A and thereby fine-tunes HCV RNA replication"  J. Biol Chem. 294, 13171-13185 (2019).
PubMed: 31315928

Assembly members:

Assembly members:
entity_1, polymer, 20 residues, 2268.570 Da.

Natural source:

Natural source:   Common Name: HCV   Taxonomy ID: 356411   Superkingdom: Viruses   Kingdom: not available   Genus/species: Hepacivirus 'Hepatitis C virus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherchia coli BL21(DE3)   Vector: pET32a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GFPRALPAWARPDYNPPLVE

Data sets:
Data typeCount
13C chemical shifts66
15N chemical shifts20
1H chemical shifts138

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 20 residues - 2268.570 Da.

1   GLYPHEPROARGALALEUPROALATRPALA
2   ARGPROASPTYRASNPROPROLEUVALGLU

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks