BMRB Entry 53357

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53357

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Title:
Partial NMR assignment of the CarD transcription factor in complex with CrsL regulator from Mycobacterium smegmatis
Deposition date:
2025-09-19
Original release date:
2025-09-23
Authors:
Cerny, Martin; Shoman, Mahmoud; Hnilicova, Jarmila; Zidek, Lukas
Citation:

Citation: Shoman, Mahmoud; Cerny, Martin; Jirat Matejckova, Jitka; Schwarz, Marek; Borah, Nabajyoti; Vankova Hausnerova, Viola; Neva, Silvia; Sikova, Michaela; Sanderova, Hana; Halada, Petr; Hubalek, Martin; Dvorakova, Vera; Prevorovsky, Martin; Holubova, Jana; Stanek, Ondrej; Krasny, Libor; Zidek, Lukas; Hnilicova, Jarmila. "Expanding the CarD interaction network: CrsL is a novel transcription regulator in actinobacteria"  Nucleic Acids Res. ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 163 residues, 17991.44 Da.
entity_2, polymer, 62 residues, 5970 Da.

Natural source:

Natural source:   Common Name: Mycobacterium smegmatis   Taxonomy ID: 1772   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycobacterium smegmatis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GMIFKVGDTVVYPHHGAALI EAIETRTIKGEQKEYLVLKV AQGDLTVRVPADNAEYVGVR DVVGQEGLDKVFQVLRAPHT EEPTNWSRRYKANLEKLASG DVNKVAEVVRDLWRRDQERG LSAGEKRMLAKARQILVGEL ALAENTDDAKAETILDEVLA AAS
entity_2: MPAKTDPADLGDVEPLADDT ASQARRVVATYATDADECRM FLSMLGIGPSKTEVLEHHHH HH

Data sets:
Data typeCount
13C chemical shifts120
15N chemical shifts67
1H chemical shifts67

Time Domain Data

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1CarD1
2CrsL2

Entities:

Entity 1, CarD 163 residues - 17991.44 Da.

1   GLYMETILEPHELYSVALGLYASPTHRVAL
2   VALTYRPROHISHISGLYALAALALEUILE
3   GLUALAILEGLUTHRARGTHRILELYSGLY
4   GLUGLNLYSGLUTYRLEUVALLEULYSVAL
5   ALAGLNGLYASPLEUTHRVALARGVALPRO
6   ALAASPASNALAGLUTYRVALGLYVALARG
7   ASPVALVALGLYGLNGLUGLYLEUASPLYS
8   VALPHEGLNVALLEUARGALAPROHISTHR
9   GLUGLUPROTHRASNTRPSERARGARGTYR
10   LYSALAASNLEUGLULYSLEUALASERGLY
11   ASPVALASNLYSVALALAGLUVALVALARG
12   ASPLEUTRPARGARGASPGLNGLUARGGLY
13   LEUSERALAGLYGLULYSARGMETLEUALA
14   LYSALAARGGLNILELEUVALGLYGLULEU
15   ALALEUALAGLUASNTHRASPASPALALYS
16   ALAGLUTHRILELEUASPGLUVALLEUALA
17   ALAALASER

Entity 2, CrsL 62 residues - 5970 Da.

1   METPROALALYSTHRASPPROALAASPLEU
2   GLYASPVALGLUPROLEUALAASPASPTHR
3   ALASERGLNALAARGARGVALVALALATHR
4   TYRALATHRASPALAASPGLUCYSARGMET
5   PHELEUSERMETLEUGLYILEGLYPROSER
6   LYSTHRGLUVALLEUGLUHISHISHISHIS
7   HISHIS

Samples:

sample_1: CrsL 1 mM; CarD, [U-100% 13C; U-100% 15N], 0.5 mM; TRIS 50 mM; sodium chloride 300 mM; sodium azide 1 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 300 mM; pH: 7.5; pressure: 1 atm; temperature: 300.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v4.0.9, 4.1.4 - collection

NMRPipe v11.2 - processing

NMRDraw - processing

NMRFAM-SPARKY v1.470 - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker AVANCE NEO 950 MHz

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