BMRB Entry 30037

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PDB ID:
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

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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
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 20 residues - 2268.570 Da.

1   GLYPHEPROARGALALEUPROALATRPALA
2   ARGPROASPTYRASNPROPROLEUVALGLU

Samples:

sample_1: NS5A-D2(JFH1)peptide 304-323, unlabelled, 5 mM; NaCl 30 mM

sample_2: 15N 13C NS5A-D2(JFH1)peptide 304-323, [U-99% 13C; U-99% 15N], 1 mM; NaCl 30 mM

sample_conditions_1: ionic strength: 30 mM; pH: 6.4; pressure: 1 bar; temperature: 298 K

sample_conditions_2: ionic strength: 30 mM; pH: 6.4; pressure: 1 bar; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1H-15N_HSQCsample_1isotropicsample_conditions_1
HNCACBsample_2isotropicsample_conditions_2
HNCOACBsample_2isotropicsample_conditions_2
HNCOsample_2isotropicsample_conditions_2
HNCACOsample_2isotropicsample_conditions_2
1H-1H TOCSYsample_1isotropicsample_conditions_1
1H-1H NOESYsample_1isotropicsample_conditions_1
1H-15N_HSQCsample_2isotropicsample_conditions_2

Software:

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation

SPARKY, Goddard - peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz

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