BMRB Entry 50780

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50780

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Title:
Partial assignment of the dimeric SARS-CoV-2 Main Protease
Deposition date:
2021-02-19
Original release date:
2021-09-28
Authors:
Boll, Emmanuelle; Cantrelle, Francois-xavier; Hanoulle, Xavier
Citation:

Citation: Cantrelle, Francois-xavier; Boll, Emmanuelle; Brier, Lucile; Moschidi, Danai; Belouzard, Sandrine; Landry, Valerie; Leroux, Florence; Dewitte, Frederique; Landrieu, Isabelle; Dubuisson, Jean; Deprez, Benoit; Charton, Julie; Hanoulle, Xavier. "NMR spectroscopy of the main protease of SARS-CoV-2 and fragment-based screening identify three protein hotspots and an antiviral fragment"  Angew. Chem. Int. Ed. Engl. 60, 25428-25435 (2021).
PubMed: 34570415

Assembly members:

Assembly members:
entity_1, polymer, 306 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: SARS-CoV-2   Taxonomy ID: 2697049   Superkingdom: Viruses   Kingdom: not available   Genus/species: Betacoronavirus HCoV-SARS

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pHIS-SUMO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SGFRKMAFPSGKVEGCMVQV TCGTTTLNGLWLDDVVYCPR HVICTSEDMLNPNYEDLLIR KSNHNFLVQAGNVQLRVIGH SMQNCVLKLKVDTANPKTPK YKFVRIQPGQTFSVLACYNG SPSGVYQCAMRPNFTIKGSF LNGSCGSVGFNIDYDCVSFC YMHHMELPTGVHAGTDLEGN FYGPFVDRQTAQAAGTDTTI TVNVLAWLYAAVINGDRWFL NRFTTTLNDFNLVAMKYNYE PLTQDHVDILGPLSAQTGIA VLDMCASLKELLQNGMNGRT ILGSALLEDEFTPFDVVRQC SGVTFQ

Data sets:
Data typeCount
13C chemical shifts680
15N chemical shifts185
1H chemical shifts185

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
13CLpro dimeric, chain 11
23CLpro dimeric, chain 21

Entities:

Entity 1, 3CLpro dimeric, chain 1 306 residues - Formula weight is not available

1   SERGLYPHEARGLYSMETALAPHEPROSER
2   GLYLYSVALGLUGLYCYSMETVALGLNVAL
3   THRCYSGLYTHRTHRTHRLEUASNGLYLEU
4   TRPLEUASPASPVALVALTYRCYSPROARG
5   HISVALILECYSTHRSERGLUASPMETLEU
6   ASNPROASNTYRGLUASPLEULEUILEARG
7   LYSSERASNHISASNPHELEUVALGLNALA
8   GLYASNVALGLNLEUARGVALILEGLYHIS
9   SERMETGLNASNCYSVALLEULYSLEULYS
10   VALASPTHRALAASNPROLYSTHRPROLYS
11   TYRLYSPHEVALARGILEGLNPROGLYGLN
12   THRPHESERVALLEUALACYSTYRASNGLY
13   SERPROSERGLYVALTYRGLNCYSALAMET
14   ARGPROASNPHETHRILELYSGLYSERPHE
15   LEUASNGLYSERCYSGLYSERVALGLYPHE
16   ASNILEASPTYRASPCYSVALSERPHECYS
17   TYRMETHISHISMETGLULEUPROTHRGLY
18   VALHISALAGLYTHRASPLEUGLUGLYASN
19   PHETYRGLYPROPHEVALASPARGGLNTHR
20   ALAGLNALAALAGLYTHRASPTHRTHRILE
21   THRVALASNVALLEUALATRPLEUTYRALA
22   ALAVALILEASNGLYASPARGTRPPHELEU
23   ASNARGPHETHRTHRTHRLEUASNASPPHE
24   ASNLEUVALALAMETLYSTYRASNTYRGLU
25   PROLEUTHRGLNASPHISVALASPILELEU
26   GLYPROLEUSERALAGLNTHRGLYILEALA
27   VALLEUASPMETCYSALASERLEULYSGLU
28   LEULEUGLNASNGLYMETASNGLYARGTHR
29   ILELEUGLYSERALALEULEUGLUASPGLU
30   PHETHRPROPHEASPVALVALARGGLNCYS
31   SERGLYVALTHRPHEGLN

Samples:

sample_1: 3CLpro dimeric, [U-13C; U-15N; U-2H], 530 uM; sodium phosphate 50 mM; sodium chloride 40 mM; EDTA 0.1 mM; D2O 5%; THP 3 mM; TSP 100 uM

sample_2: 3CLpro dimeric, [U-13C; U-15N; U-2H], 530 uM; sodium phosphate 50 mM; sodium chloride 40 mM; EDTA 0.1 mM; D2O 5%; THP 3 mM; TSP 100 uM; Boceprevir 2 mM; DMSO 3%

sample_3: 3CLpro dimeric, [U-13C; U-15N; U-2H], 440 uM; sodium phosphate 50 mM; sodium chloride 40 mM; EDTA 0.1 mM; D2O 5%; THP 3 mM; TSP 100 uM

sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 305 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCACB TROSYsample_1isotropicsample_conditions_1
3D HN(CO)CACB TROSYsample_1isotropicsample_conditions_1
3D HNCO TROSYsample_1isotropicsample_conditions_1
3D HN(CA)CO TROSYsample_1isotropicsample_conditions_1
3D HN(CO)CA TROSYsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_2isotropicsample_conditions_1
3D HNCACB TROSYsample_2isotropicsample_conditions_1
3D HN(CO)CACB TROSYsample_2isotropicsample_conditions_1
2D 1H-15N TROSYsample_3isotropicsample_conditions_1
3D HNCACB TROSYsample_3isotropicsample_conditions_1
3D HN(CO)CACB TROSYsample_3isotropicsample_conditions_1
3D HNCO TROSYsample_3isotropicsample_conditions_1

Software:

TOPSPIN v4.07 - collection

NMRPipe - processing

qMDD - processing

CcpNMR v2.5.1 - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker AVANCE NEO 900 MHz

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