BMRB Entry 31264

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31264

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Title:
NMR RDC refinement of the catalytic domain of the SARS-CoV-2 monomeric Main Protease (MPROH41Q,10-306)
Deposition date:
2025-08-08
Original release date:
2025-09-25
Authors:
Smith, M.; Ying, J.; Shen, Y.; Louis, J.; Bax, A.
Citation:

Citation: Smith, M.; Ying, J.; Yang, S.; Louis, J.; Bax, A.. "Solution Domain Dynamics of Monomeric SARS-CoV-2 Main Pro-tease Revealed by Optimized NMR Residual Dipolar Coupling Measurements."  .

Assembly members:

Assembly members:
entity_1, polymer, 306 residues, 33815.527 Da.

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

Entity Sequences (FASTA):

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

Data sets:
Data typeCount
13C chemical shifts237
15N chemical shifts136
1H chemical shifts136

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 306 residues - 33815.527 Da.

1   SERGLYPHEARGLYSMETALAPHEPROSER
2   GLYLYSVALGLUGLYCYSMETVALGLNVAL
3   THRCYSGLYTHRTHRTHRLEUASNGLYLEU
4   TRPLEUASPASPVALVALTYRCYSPROARG
5   GLNVALILECYSTHRSERGLUASPMETLEU
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: sodium chloride 20 mM; sodium azide 0.02%; HEPES 25 mM; TCEP 1 mM; MPro(10,306,H41Q), [U-13C; U-15N; U-2H], 500 uM

sample_2: sodium chloride 20 mM; sodium azide 0.02%; HEPES 25 mM; TCEP 1 mM; MPro(10,306,H41Q), [U-13C; U-15N; U-2H], 430 uM; Pf1 phage 13 mg/mL

sample_conditions_1: ionic strength: 20 mM; pH: 6.9; pressure: 1 bar; temperature: 288 K

sample_conditions_2: ionic strength: 20 mM; pH: 6.9; pressure: 1 bar; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSY-HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
4D 1H-15N TROSY-NOESY-TROSYsample_1isotropicsample_conditions_1
2D 1H-15N ARTSYsample_2anisotropicsample_conditions_2
2D 15-15N QJNC' TROSYsample_2anisotropicsample_conditions_2
3D TATER-HNCOsample_2anisotropicsample_conditions_2
3D QJC'CA HNCOsample_2anisotropicsample_conditions_2
3D ARTSY-HNCOsample_2anisotropicsample_conditions_2

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CcpNmr Analysis, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE NEO 800 MHz
  • Bruker AVANCE NEO 600 MHz

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