BMRB Entry 30926

Title:
Solution NMR structure of peptidase domain from Clostridium thermocellum PCAT1
Deposition date:
2021-06-13
Original release date:
2021-12-31
Authors:
Bhattacharya, S.; Palillo, A.
Citation:

Citation: Bhattacharya, S.; Pallilo, A.. "Structural and dynamic studies of the peptidase domain from Clostridium thermocellum PCAT1"  Protein Sci. 31, 498-512 (2022).
PubMed: 34865273

Assembly members:

Assembly members:
entity_1, polymer, 151 residues, 16635.389 Da.

Natural source:

Natural source:   Common Name: Clostridium thermocellum   Taxonomy ID: 203119   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Clostridium thermocellum

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pMSCG20

Data sets:
Data typeCount
13C chemical shifts622
15N chemical shifts151
1H chemical shifts1057

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 151 residues - 16635.389 Da.

1   SERASNALAMETLEUARGARGLEUPHELYS
2   LYSLYSTYRVALCYSVALARGGLNTYRASP
3   LEUTHRASPALAGLYALAALACYSLEUSER
4   SERILEALAGLNTYRTYRGLYLEULYSMET
5   SERLEUALALYSILEARGGLUMETTHRGLY
6   THRASPTHRGLNGLYTHRASNALATYRGLY
7   LEUILEHISALAALALYSGLNLEUGLYPHE
8   SERALALYSGLYVALLYSALASERLYSGLU
9   ASPLEULEULYSASPPHEARGLEUPROALA
10   ILEALAASNVALILEVALASPASNARGLEU
11   ALAHISPHEVALVALILETYRSERILELYS
12   ASNARGILEILETHRVALALAASPPROGLY
13   LYSGLYILEVALARGTYRSERMETASPASP
14   PHECYSSERILETRPTHRGLYGLYLEUVAL
15   LEULEUGLUPROGLYGLUALAPHEGLNLYS
16   GLY

Samples:

sample_1: C39 peptidase domain, [U-100% 13C; U-100% 15N], 675 uM; sodium phosphate 50 uM; sodium chloride 150 uM; DTT 5 mM; PBS buffer 50 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

TopSpin v2.1, 3.5, Bruker Biospin - collection

TopSpin v2.1, 3.6, Bruker Biospin - processing

CARA v1.5, Keller and Wuthrich - chemical shift assignment, peak picking

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

ARIA v2.3, Linge, O'Donoghue and Nilges - refinement

NMR spectrometers:

  • Bruker AVANCE 900.03 MHz
  • Bruker AVANCE III HD 800.23 MHz

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