BMRB Entry 52547

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52547

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

Title:
Solution NMR assignment of Coxsackievirus B3 (CVB3) 3C protease
Deposition date:
2024-07-11
Original release date:
2024-11-05
Authors:
De Santis, Alessia; Orsetti, Andrea; Grifagni, Deborah; Lenci, Elena; Cantini, Francesca; Calderone, Vito; Trabocchi, Andrea; Ciofi-Baffoni, Simone; Rosato, Antonio; D'Onofrio, Mariapina
Citation:

Citation: De Santis, Alessia; Grifagni, Deborah; Orsetti, Andrea; Lenci, Elena; Rosato, Antonio; D'Onofrio, Mariapina; Trabocchi, Andrea; Ciofi-Baffoni, Simone; Cantini, Francesca; Calderone, Vito. "A Structural Investigation of the Interaction between a GC-376-Based Peptidomimetic PROTAC and Its Precursor with the Viral Main Protease of Coxsackievirus B3"  Biomolecules 14, 1260-1260 (2024).
PubMed: 39456193

Assembly members:

Assembly members:
entity_1, polymer, 192 residues, Formula weight is not available
entity_2, non-polymer, 459.54 Da.

Natural source:

Natural source:   Common Name: Enterovirus Coxsackievirus B3   Taxonomy ID: 12072   Superkingdom: Viruses   Kingdom: not available   Genus/species: Enterovirus Enterovirus B

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-24a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGPAFEFAVAMMKRNSSTVK TEYGEFTMLGIYDRWAVLPR HAKPGPTILMNDQEVGVLDA KELVDKDGTNLELTLLKLNR NEKFRDIRGFLAKEEVEVNE AVLAINTSKFPNMYIPVGQV TEYGFLNLGGTPTKRMLMYN FPTRAGQCGGVLMSTGKVLG IHVGGNGHQGFSAALLKHYF NDEQLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts516
15N chemical shifts189
1H chemical shifts618

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CVB3 3CPro1
2FT2342

Entities:

Entity 1, CVB3 3CPro 192 residues - Formula weight is not available

G2 corresponds to G1541 in the full length sequence (strain Nancy UNIPROT Entry : P03313 * POLG_CXB3N).

1   METGLYPROALAPHEGLUPHEALAVALALA
2   METMETLYSARGASNSERSERTHRVALLYS
3   THRGLUTYRGLYGLUPHETHRMETLEUGLY
4   ILETYRASPARGTRPALAVALLEUPROARG
5   HISALALYSPROGLYPROTHRILELEUMET
6   ASNASPGLNGLUVALGLYVALLEUASPALA
7   LYSGLULEUVALASPLYSASPGLYTHRASN
8   LEUGLULEUTHRLEULEULYSLEUASNARG
9   ASNGLULYSPHEARGASPILEARGGLYPHE
10   LEUALALYSGLUGLUVALGLUVALASNGLU
11   ALAVALLEUALAILEASNTHRSERLYSPHE
12   PROASNMETTYRILEPROVALGLYGLNVAL
13   THRGLUTYRGLYPHELEUASNLEUGLYGLY
14   THRPROTHRLYSARGMETLEUMETTYRASN
15   PHEPROTHRARGALAGLYGLNCYSGLYGLY
16   VALLEUMETSERTHRGLYLYSVALLEUGLY
17   ILEHISVALGLYGLYASNGLYHISGLNGLY
18   PHESERALAALALEULEULYSHISTYRPHE
19   ASNASPGLUGLNLEUGLUHISHISHISHIS
20   HISHIS

Entity 2, FT234 - C24 H33 N3 O6 - 459.54 Da.

Samples:

sample_1: CVB3 3CPro, [U-99% 13C; U-99% 15N], 0.2 mM; CVB3 3CPro, [U-99% 15N], 0.2 mM; FT234 0.2 mM; sodium phosphate 50 mM; sodium chloride 100 mM; L -Glutamic acid 50 mM; L-arginine 50 mM; DTT 1 mM; EDTA 1 mM; d3-acetonitrile, [U-100% 2H], 1.6%

sample_conditions_1: ionic strength: 100 mM; pH: 6; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D CBCACONHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

CARA v1.8 - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE NEO 500 MHz
  • Bruker AVANCE III 950 MHz

Related Database Links:

UNIPROT P03313 * POLG_CXB3N

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