BMRB Entry 17911

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17911
MolProbity Validation Chart

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Title:
C-terminal domain of SARS-CoV main protease
Deposition date:
2011-09-02
Original release date:
2012-09-04
Authors:
Xia, Bin; Kang, Xue
Citation:

Citation: Xia, Bin. "NMR solution structure of C-terminal domain of SARS-CoV main protease in 2.5M urea"  .

Assembly members:

Assembly members:
Mpro-C, polymer, 120 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: SARS coronavirus   Taxonomy ID: 227859   Superkingdom: Viruses   Kingdom: not available   Genus/species: SARS coronavirus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Mpro-C: DRQTAQAAGTDTTITLNVLA WLYAAVINGDRWFLNRFTTT LNDFNLVAMKYNYEPLTQDH VDILGPLSAQTGIAVLDMCA ALKELLQNGMNGRTILGSTI LEDEFTPFDVVRQCSGVTFQ

Data sets:
Data typeCount
13C chemical shifts360
15N chemical shifts130
1H chemical shifts795

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Mpro-C1

Entities:

Entity 1, Mpro-C 120 residues - Formula weight is not available

1   ASPARGGLNTHRALAGLNALAALAGLYTHR
2   ASPTHRTHRILETHRLEUASNVALLEUALA
3   TRPLEUTYRALAALAVALILEASNGLYASP
4   ARGTRPPHELEUASNARGPHETHRTHRTHR
5   LEUASNASPPHEASNLEUVALALAMETLYS
6   TYRASNTYRGLUPROLEUTHRGLNASPHIS
7   VALASPILELEUGLYPROLEUSERALAGLN
8   THRGLYILEALAVALLEUASPMETCYSALA
9   ALALEULYSGLULEULEUGLNASNGLYMET
10   ASNGLYARGTHRILELEUGLYSERTHRILE
11   LEUGLUASPGLUPHETHRPROPHEASPVAL
12   VALARGGLNCYSSERGLYVALTHRPHEGLN

Samples:

sample_1: Mpro-C, [U-100% 15N], 1 mM; Mpro-C, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%; DTT 1 mM; PBS 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - structure solution

NMRView, Johnson, One Moon Scientific - chemical shift assignment

ProcheckNMR, Laskowski and MacArthur - processing

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

SANE, Duggan, Legge, Dyson & Wright - structure solution

TALOS, Cornilescu, Delaglio and Bax - structure solution

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAC81346 BAC81347 BAC81360 BAC81361 BAC81374
GB AAP13439 AAP13442 AAP13566 AAP13575 AAP30028
REF NP_828849 NP_828850 NP_828863
SP P0C6F5 P0C6F8 P0C6T7 P0C6U8 P0C6V9
AlphaFold P0C6F5 P0C6F8 P0C6T7 P0C6U8 P0C6V9

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