BMRB Entry 50371

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR50371

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Title:
Backbone assigenments of the Lon protease from Mycobacterium tuberculosis complex
Deposition date:
2020-07-01
Original release date:
2020-08-04
Authors:
Zhang, Qiaodong; Bi, Fangkai
Citation:

Citation: Zhang, Qiaodong; Bi, Fangkai. "Backbone assignments of the Lon protease from Mycobacterium tuberculosis complex"  .

Assembly members:

Assembly members:
entity_1, polymer, 211 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Mycobacterium tuberculosis   Taxonomy ID: 1773   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycobacterium tuberculosis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: E. coli - cell free   Vector: pSUMO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MDLELSMSETLTLPVLPLED GVVLPGMVVPLDLSENGEVR AAIEAARAAAQSRGPGIRSV SKPRVLLVPRLNGRYADVGT LGVIEQEGRLPGGEPGAVVR GVSRVRIGTGTTGPGAALWV EGTVLEAPPASGRAQELAKE YKGLVSAILQKRGAWQVVDV VQQIDDPSTLADNSGYAPYL TDEQKIEVLETVDVVERLEL VIGWTRDHLAE

Data sets:
Data typeCount
13C chemical shifts528
15N chemical shifts181
1H chemical shifts181

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1lon 2111

Entities:

Entity 1, lon 211 211 residues - Formula weight is not available

1   METASPLEUGLULEUSERMETSERGLUTHR
2   LEUTHRLEUPROVALLEUPROLEUGLUASP
3   GLYVALVALLEUPROGLYMETVALVALPRO
4   LEUASPLEUSERGLUASNGLYGLUVALARG
5   ALAALAILEGLUALAALAARGALAALAALA
6   GLNSERARGGLYPROGLYILEARGSERVAL
7   SERLYSPROARGVALLEULEUVALPROARG
8   LEUASNGLYARGTYRALAASPVALGLYTHR
9   LEUGLYVALILEGLUGLNGLUGLYARGLEU
10   PROGLYGLYGLUPROGLYALAVALVALARG
11   GLYVALSERARGVALARGILEGLYTHRGLY
12   THRTHRGLYPROGLYALAALALEUTRPVAL
13   GLUGLYTHRVALLEUGLUALAPROPROALA
14   SERGLYARGALAGLNGLULEUALALYSGLU
15   TYRLYSGLYLEUVALSERALAILELEUGLN
16   LYSARGGLYALATRPGLNVALVALASPVAL
17   VALGLNGLNILEASPASPPROSERTHRLEU
18   ALAASPASNSERGLYTYRALAPROTYRLEU
19   THRASPGLUGLNLYSILEGLUVALLEUGLU
20   THRVALASPVALVALGLUARGLEUGLULEU
21   VALILEGLYTRPTHRARGASPHISLEUALA
22   GLU

Samples:

sample_1: the Lon protease fragment (1-211), [U-100% 13C; U-100% 15N], 11.7965 ± 0.236 mg/mL; the Lon protease fragment (1-211), [U-100% 13C; U-100% 15N], 11.7965 ± 0.236 mg/mL; the Lon protease fragment (1-211), [U-100% 13C; U-100% 15N], 11.7965 ± 0.236 mg/mL

sample_conditions_1: ionic strength: 0.0005 M; pH: 6.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1D 1Hsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

SPARKY - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 850 MHz

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