BMRB Entry 52381

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52381

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Chemical shift assignments of the BCCP domain of Propionyl CoA carboxylase of Leishmania major
Deposition date:
2024-04-01
Original release date:
2024-12-26
Authors:
Bhatnagar, Sonika; Sundd, Monica
Citation:

Citation: Bhatnagar, Sonika; Sadhukhan, Debodyuti; Sundd, Monica. "Backbone assignments of the biotin carboxyl carrier protein domain of Propionyl CoA carboxylase of Leishmania major and its interaction with its cognate Biotin protein ligase"  Biomol. NMR Assign. 18, 309-314 (2024).
PubMed: 39313636

Assembly members:

Assembly members:
entity_1, polymer, 74 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Leishmania major   Taxonomy ID: 5664   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Leishmania major

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MTVNTKQILSPMPGVIVAIK VQPGQTVVAGEELLTLEAMK MRNKIHAQADGKVKEIKVTL GATVEDSEVLVELE

Data sets:
Data typeCount
13C chemical shifts245
15N chemical shifts67
1H chemical shifts64

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BCCP domain of Propionyl CoA carboxylase1

Entities:

Entity 1, BCCP domain of Propionyl CoA carboxylase 74 residues - Formula weight is not available

1   METTHRVALASNTHRLYSGLNILELEUSER
2   PROMETPROGLYVALILEVALALAILELYS
3   VALGLNPROGLYGLNTHRVALVALALAGLY
4   GLUGLULEULEUTHRLEUGLUALAMETLYS
5   METARGASNLYSILEHISALAGLNALAASP
6   GLYLYSVALLYSGLUILELYSVALTHRLEU
7   GLYALATHRVALGLUASPSERGLUVALLEU
8   VALGLULEUGLU

Samples:

sample_1: Biotin carboxyl carrier protein domain, [U-99% 13C; U-99% 15N], 0.9 mM; Tris 50 mM; NaCl 100 mM

sample_conditions_1: ionic strength: 150 mM; pH: 8.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1

Software:

CARA vlinux - chemical shift assignment

NMRPipe vlinux - processing

NMR spectrometers:

  • Bruker AVANCE III 700 MHz

Related Database Links:

UNP E9ABZ4

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