BMRB Entry 51488

Title:
Backbone assignment of the LCC PETase   PubMed: 35794828
Deposition date:
2022-06-13
Original release date:
2022-08-08
Authors:
Charlier, Cyril; Lippens, Guy
Citation:

Citation: Charlier, Cyril; Gavalda, Sabine; Borsenberger, Vinciane; Duquesne, Sophie; Marty, Alain; Tournier, Vincent; Lippens, Guy. "An NMR look at an engineered PET depolymerase"  Biophys. J. 121, 2882-2894 (2022).

Assembly members:

Assembly members:
entity_1, polymer, 258 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: uncultured bacterium   Taxonomy ID: 77133   Superkingdom: Bacteria   Kingdom: not available   Genus/species: uncultured bacterium

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-26b

Experimental source:

Natural source:   Common Name: uncultured bacterium   Taxonomy ID: 77133   Superkingdom: Bacteria   Kingdom: not available   Genus/species: uncultured bacterium

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-26b

Data sets:
Data typeCount
13C chemical shifts647
15N chemical shifts204
1H chemical shifts204

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1LCC PETase1

Entities:

Entity 1, LCC PETase 258 residues - Formula weight is not available

1   SERASNPROTYRGLNARGGLYPROASNPRO
2   THRARGSERALALEUTHRALAASPGLYPRO
3   PHESERVALALATHRTYRTHRVALSERARG
4   LEUSERVALSERGLYPHEGLYGLYGLYVAL
5   ILETYRTYRPROTHRGLYTHRSERLEUTHR
6   PHEGLYGLYILEALAMETSERPROGLYTYR
7   THRALAASPALASERSERLEUALATRPLEU
8   GLYARGARGLEUALASERHISGLYPHEVAL
9   VALLEUVALILEASNTHRASNSERARGPHE
10   ASPTYRPROASPSERARGALASERGLNLEU
11   SERALAALALEUASNTYRLEUARGTHRSER
12   SERPROSERALAVALARGALAARGLEUASP
13   ALAASNARGLEUALAVALALAGLYHISALA
14   METGLYGLYGLYGLYTHRLEUARGILEALA
15   GLUGLNASNPROSERLEULYSALAALAVAL
16   PROLEUTHRPROTRPHISTHRASPLYSTHR
17   PHEASNTHRSERVALPROVALLEUILEVAL
18   GLYALAGLUALAASPTHRVALALAPROVAL
19   SERGLNHISALAILEPROPHETYRGLNASN
20   LEUPROSERTHRTHRPROLYSVALTYRVAL
21   GLULEUASPASNALASERHISPHEALAPRO
22   ASNSERASNASNALAALAILESERVALTYR
23   THRILESERTRPMETLYSLEUTRPVALASP
24   ASNASPTHRARGTYRARGGLNPHELEUCYS
25   ASNVALASNASPPROALALEUSERASPPHE
26   ARGTHRASNASNARGHISCYSGLN

Samples:

sample_1: LCC inactive mutant (S165A), [U-98% 13C; U-98% 15N], 600 uM; Tris-HCl 25 mM; NaCl 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
1D 1Hsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1

Software:

NMRFAM-SPARKY - chemical shift assignment

TOPSPIN v3.5pl6 - collection

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

Related Database Links:

PDB

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