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BMRB Entry 51471

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51471

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Title: ADPr bound macro domain of Hepatitis E virus   PubMed: 36272047

Deposition date: 2022-05-23 Original release date: 2022-10-28

Authors: Politi, Maria; Gallo, Angelo; Spyroulias, Georgios

Citation: Politi, Maria; Gallo, Angelo; Bouras, Georgios; Birkou, Maria; Canard, Bruno; Coutard, Bruno; Spyroulias, Georgios. "1H, 13C, 15N backbone resonance assignment of apo and ADP-ribose bound forms of the macro domain of Hepatitis E virus through solution NMR spectroscopy"  Biomol. NMR Assignments 17, 1-8 (2022).

Assembly members:
entity_1, polymer, 163 residues, Formula weight is not available
entity_APR, non-polymer, 559.316 Da.

Natural source:   Common Name: Hepatitis E virus   Taxonomy ID: 1678143   Superkingdom: Viruses   Kingdom: not available   Genus/species: Orthohepevirus Orthohepevirus A

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET20b(+)

Entity Sequences (FASTA):
entity_1: MHQAARHRRLLFTYPDGSKV FAGSLFESTCTWLVNASNVD HRPGGGLCHAFYQRYPASFD AASFVMRDGAAAYTLTPRPI IHAVAPDYRLEHNPKMLEAA YRETCSRLGTAAYPLLGTGI YQVPIGPSFDAWERNHRPGD ELYLPELAARWFEANLEHHH HHH

Data sets:
Data typeCount
13C chemical shifts618
15N chemical shifts146
1H chemical shifts874

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MD HEV1
2ADPr2

Entities:

Entity 1, MD HEV 163 residues - Formula weight is not available

The cloned plasmid attached to the native protein presents one artificial N-terminal residue (M-1), two C-terminal residues (LE) and six histidines.

1   METHISGLNALAALAARGHISARGARGLEU
2   LEUPHETHRTYRPROASPGLYSERLYSVAL
3   PHEALAGLYSERLEUPHEGLUSERTHRCYS
4   THRTRPLEUVALASNALASERASNVALASP
5   HISARGPROGLYGLYGLYLEUCYSHISALA
6   PHETYRGLNARGTYRPROALASERPHEASP
7   ALAALASERPHEVALMETARGASPGLYALA
8   ALAALATYRTHRLEUTHRPROARGPROILE
9   ILEHISALAVALALAPROASPTYRARGLEU
10   GLUHISASNPROLYSMETLEUGLUALAALA
11   TYRARGGLUTHRCYSSERARGLEUGLYTHR
12   ALAALATYRPROLEULEUGLYTHRGLYILE
13   TYRGLNVALPROILEGLYPROSERPHEASP
14   ALATRPGLUARGASNHISARGPROGLYASP
15   GLULEUTYRLEUPROGLULEUALAALAARG
16   TRPPHEGLUALAASNLEUGLUHISHISHIS
17   HISHISHIS

Entity 2, ADPr - C15 H23 N5 O14 P2 - 559.316 Da.

1   APR

Samples:

sample_1: MD HEV, [U-99% 13C; U-99% 15N], 0.5 mM; D2O, [U-2H], 10%; APR 5 mM; DSS 0.25 mM; EDTA 5 mM; sodium acetate 10 mM; H2O 90%

sample_conditions_1: ionic strength: 10 mM; pH: 5.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1D 1Hsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCACONHsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v4.1.1 - collection, processing

CARA - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker AVANCE III 700 MHz

Related Database Links:

Uniprot P29324
AlphaFold Q81873

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