BMRB Entry 52399

Title:
BRCT1
Deposition date:
2024-04-15
Original release date:
2024-06-19
Authors:
Vu, Duc Duy; Pelupessy, Philippe; Wang, Ziqing; Carlier, Ludovic; Bouvignies, Guillaume; Ferrage, Fabien
Citation:

Citation: Vu, Duc-Duy; Bonucci, Alessio; Breniere, Manon; Cisneros-Aguirre, Metztli; Pelupessy, Philippe; Wang, Ziqing; Carlier, Ludovic; Bouvignies, Guillaume; Cortes, Patricia; Aggarwal, Aneel; Blackledge, Martin; Gueroui, Zoher; Belle, Valerie; Stark, Jeremy; Modesti, Mauro; Ferrage, Fabien. "Multivalent interactions of the disordered regions of XLF and XRCC4 foster robust cellular NHEJ and drive the formation of ligation-boosting condensates in vitro"  Nat. Struct. Mol. Biol. ., .-. (2024).

Assembly members:

Assembly members:
entity_1, polymer, 109 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pMAL-c5x

Data sets:
Data typeCount
13C chemical shifts309
15N chemical shifts98
1H chemical shifts99

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BRCT11

Entities:

Entity 1, BRCT1 109 residues - Formula weight is not available

1   SERGLYSERLYSILESERASNILEPHEGLU
2   ASPVALGLUPHECYSVALMETSERGLYTHR
3   ASPSERGLNPROLYSPROASPLEUGLUASN
4   ARGILEALAGLUPHEGLYGLYTYRILEVAL
5   GLNASNPROGLYPROASPTHRTYRCYSVAL
6   ILEALAGLYSERGLUASNILEARGVALLYS
7   ASNILEILELEUSERASNLYSHISASPVAL
8   VALLYSPROALATRPLEULEUGLUCYSPHE
9   LYSTHRLYSSERPHEVALPROTRPGLNPRO
10   ARGPHEMETILEHISMETCYSPROSERTHR
11   LYSGLUHISPHEALAARGGLUTYRASP

Samples:

sample_1: BRCT1, [U-100% 13C; U-100% 15N], 400-500 uM; Bistris 6.5 20 mM; potassium chloride 150 mM; EDTA 1 mM; DTT 1 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

SPARKY - chemical shift assignment

TOPSPIN - collection

NMR spectrometers:

  • Bruker AVANCE NEO 800 MHz

Related Database Links:

UNP P49917

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