BMRB Entry 52237

Title:
1H, 13C and 15N backbone and sidechain assignment of the BRCT domain of Mtb LigA
Deposition date:
2023-12-12
Original release date:
2024-01-15
Authors:
Vaishnav, Jayanti; Ampapathi, Ravi
Citation:

Citation: Vaishnav, Jayanti; Ampapathi, Ravi. "1H, 15N and 13C resonance backbone and side-chain assignments and secondary structure determination of the BRCT domain of Mtb LigA"  Biomol. NMR Assign. 18, 105-109 (2024).
PubMed: 38689205

Assembly members:

Assembly members:
entity_1, polymer, 116 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 DNA Technology for Protein expression   Host organism: Escherichia coli

Data sets:
Data typeCount
13C chemical shifts340
15N chemical shifts84
1H chemical shifts556

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BRCT1

Entities:

Entity 1, BRCT 116 residues - Formula weight is not available

Residues 1-16 i.e., first sixteen residues are from cloning vector; D17 to T103 in provided sequence is BRCT domain corresponding to native sequence for BRCT domain of M.tb LigA that starts from ASP 605 and runs uptil THR 691. Residues K104 to H116 are again from cloning vector containing 6X-HIS tag.

1   METALASERMETTHRGLYGLYGLNGLNMET
2   GLYARGGLYSERGLUPHEASPGLUSERVAL
3   PROARGTHRLEUALAGLYLEUTHRILEVAL
4   VALTHRGLYSERLEUTHRGLYPHESERARG
5   ASPASPALALYSGLUALAILEVALALAARG
6   GLYGLYLYSALAALAGLYSERVALSERLYS
7   LYSTHRASNTYRVALVALALAGLYASPSER
8   PROGLYSERLYSTYRASPLYSALAVALGLU
9   LEUGLYVALPROILELEUASPGLUASPGLY
10   PHEARGARGLEULEUALAASPGLYPROALA
11   SERARGTHRLYSLEUALAALAALALEUGLU
12   HISHISHISHISHISHIS

Samples:

sample_1: BRCT, [U-15N], 0.3 mM; TRIS, [U-2H], 50 mM; NaCl 200 mM; sodium azide 0.5 mM

sample_2: BRCT, [U-13C; U-15N], 0.3 mM; TRIS, [U-2H], 50 mM; NaCl 200 mM; sodium azide 0.5 mM

sample_3: BRCT, [U-13C; U-15N], 0.3 mM; TRIS, [U-2H], 50 mM; NaCl 200 mM; sodium azide 0.5 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 293.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D HCCH-COSYsample_3isotropicsample_conditions_1
3D CCH-TOCSYsample_3isotropicsample_conditions_1

Software:

NMRDraw - processing

NMRPipe - processing

NMRFAM-SPARKY - chemical shift assignment

NMR spectrometers:

  • Agilent DD2 700 MHz

Related Database Links:

Uniprot P9WNV1

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