BMRB Entry 25665

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25665

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Title:
1H, 13C, and 15N Resonance Assignments of an Enzymatically Active Domain from the Catalytic Component (CDTa) of a Clostridium difficile Binary Toxin
Deposition date:
2015-06-17
Original release date:
2016-04-21
Authors:
Roth, Braden; Weber, David; Rustandi, Richard; Ruiz, Raquel; Varney, Kristen
Citation:

Citation: Roth, Braden; Ruiz, Raquel; Varney, Kristen; Rustandi, Richard; Weber, David. "(1)H, (13)C, and (15)N resonance assignments of an enzymatically active domain from the catalytic component (CDTa, residues 216-420) of a binary toxin from Clostridium difficile"  J. Biomol. NMR 10, 213-217 (2016).
PubMed: 26886352

Assembly members:

Assembly members:
cMSD1, polymer, 205 residues, 22723.4955 Da.

Natural source:

Natural source:   Common Name: Clostridium difficile   Taxonomy ID: 1496   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Clostridium difficile

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pSUMO(Kan)-cMSD1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
cMSD1: SSLDFKDDVSKGDSWGKANY NDWSNKLTPNELADVNDYMR GGYTAINNYLISNGPVNNPN PELDSKITNIENALKREPIP TNLTVYRRSGPQEFGLTLTS PEYDFNKLENIDAFKSKWEG QALSYPNFISTSIGSVNMSA FAKRKIVLRITIPKGSPGAY LSAIPGYAGEYEVLLNHGSK FKINKIDSYKDGTITKLIVD ATLIP

Data typeCount
13C chemical shifts734
15N chemical shifts176
1H chemical shifts331

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1cMSD11

Entities:

Entity 1, cMSD1 205 residues - 22723.4955 Da.

1   SERSERLEUASPPHELYSASPASPVALSER
2   LYSGLYASPSERTRPGLYLYSALAASNTYR
3   ASNASPTRPSERASNLYSLEUTHRPROASN
4   GLULEUALAASPVALASNASPTYRMETARG
5   GLYGLYTYRTHRALAILEASNASNTYRLEU
6   ILESERASNGLYPROVALASNASNPROASN
7   PROGLULEUASPSERLYSILETHRASNILE
8   GLUASNALALEULYSARGGLUPROILEPRO
9   THRASNLEUTHRVALTYRARGARGSERGLY
10   PROGLNGLUPHEGLYLEUTHRLEUTHRSER
11   PROGLUTYRASPPHEASNLYSLEUGLUASN
12   ILEASPALAPHELYSSERLYSTRPGLUGLY
13   GLNALALEUSERTYRPROASNPHEILESER
14   THRSERILEGLYSERVALASNMETSERALA
15   PHEALALYSARGLYSILEVALLEUARGILE
16   THRILEPROLYSGLYSERPROGLYALATYR
17   LEUSERALAILEPROGLYTYRALAGLYGLU
18   TYRGLUVALLEULEUASNHISGLYSERLYS
19   PHELYSILEASNLYSILEASPSERTYRLYS
20   ASPGLYTHRILETHRLYSLEUILEVALASP
21   ALATHRLEUILEPRO

Samples:

13C15N-cMSD1: cMSD1, [U-99% 13C; U-99% 15N], 0.4 mM; H2O 90%; D2O 10%; Sodium Azide 0.02%; Hepes 15 mM; NaCl 50 mM; DTT 5 mM; EDTA 50 mM

15N-cMSD1: cMSD1, [U-99% 13C; U-99% 15N], 0.4 mM; H2O 90%; D2O 10%; Sodium Azide 0.02%; Hepes 15 mM; NaCl 50 mM; DTT 5 mM; EDTA 50 mM

cMSD1_1: ionic strength: 0.065 M; pH: 7.000; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACB13C15N-cMSD1isotropiccMSD1_1
2D 1H-15N HSQC/HMQC15N-cMSD1isotropiccMSD1_1
3D HNCO13C15N-cMSD1isotropiccMSD1_1
CBCACONH (H[N[co[{CA|ca[C]}]]])13C15N-cMSD1isotropiccMSD1_1
3D HNCA13C15N-cMSD1isotropiccMSD1_1
HNcaCO (HNcaCO)13C15N-cMSD1isotropiccMSD1_1
HNcoCA (H[N[co[{CA|ca[C]}]]])13C15N-cMSD1isotropiccMSD1_1
3D C(CO)NH13C15N-cMSD1isotropiccMSD1_1
3D HNHA13C15N-cMSD1isotropiccMSD1_1

Software:

CcpNmr_Analysis v2.4, CCPN - resonance assignment

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 950 MHz
  • Bruker Avance 600 MHz

Related Database Links:

UniProt Q9KH42
AlphaFold Q9KH42

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