BMRB Entry 52387

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52387

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

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments of the C-terminal region of XLF in the full-length XLF protein
Deposition date:
2024-04-08
Original release date:
2024-06-19
Authors:
VU, Duc Duy; 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, 299 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: pET16

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MEELEQGLLMQPWAWLQLAE NSLLAKVFITKQGYALLVSD LQQVWHEQVDTSVVSQRAKE LNKRLTAPPAAFLCHLDNLL RPLLKDAAHPSEATFSCDCV ADALILRVRSELSGLPFYWN FHCMLASPSLVSQHLIRPLM GMSLALQCQVRELATLLHMK DLEIQDYQESGATLIRDRLK TEPFEENSFLEQFMIEKLPE ACSIGDGKPFVMNLQDLYMA VTTQEVQVGQKHQGAGDPHT SNSASLQGIDSQCVNQPEQL VSSAPTLSAPEKESTGTSGP LQRPQLSKVKRKKPRGLFS

Data sets:
Data typeCount
13C chemical shifts175
15N chemical shifts61
1H chemical shifts61

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1XLF1

Entities:

Entity 1, XLF 299 residues - Formula weight is not available

1   METGLUGLULEUGLUGLNGLYLEULEUMET
2   GLNPROTRPALATRPLEUGLNLEUALAGLU
3   ASNSERLEULEUALALYSVALPHEILETHR
4   LYSGLNGLYTYRALALEULEUVALSERASP
5   LEUGLNGLNVALTRPHISGLUGLNVALASP
6   THRSERVALVALSERGLNARGALALYSGLU
7   LEUASNLYSARGLEUTHRALAPROPROALA
8   ALAPHELEUCYSHISLEUASPASNLEULEU
9   ARGPROLEULEULYSASPALAALAHISPRO
10   SERGLUALATHRPHESERCYSASPCYSVAL
11   ALAASPALALEUILELEUARGVALARGSER
12   GLULEUSERGLYLEUPROPHETYRTRPASN
13   PHEHISCYSMETLEUALASERPROSERLEU
14   VALSERGLNHISLEUILEARGPROLEUMET
15   GLYMETSERLEUALALEUGLNCYSGLNVAL
16   ARGGLULEUALATHRLEULEUHISMETLYS
17   ASPLEUGLUILEGLNASPTYRGLNGLUSER
18   GLYALATHRLEUILEARGASPARGLEULYS
19   THRGLUPROPHEGLUGLUASNSERPHELEU
20   GLUGLNPHEMETILEGLULYSLEUPROGLU
21   ALACYSSERILEGLYASPGLYLYSPROPHE
22   VALMETASNLEUGLNASPLEUTYRMETALA
23   VALTHRTHRGLNGLUVALGLNVALGLYGLN
24   LYSHISGLNGLYALAGLYASPPROHISTHR
25   SERASNSERALASERLEUGLNGLYILEASP
26   SERGLNCYSVALASNGLNPROGLUGLNLEU
27   VALSERSERALAPROTHRLEUSERALAPRO
28   GLULYSGLUSERTHRGLYTHRSERGLYPRO
29   LEUGLNARGPROGLNLEUSERLYSVALLYS
30   ARGLYSLYSPROARGGLYLEUPHESER

Samples:

sample_1: XLF, [U-100% 13C; U-100% 15N], 250 ± 10 uM; DTT 1 mM; potassium chloride 150 mM; Bistris 20 mM; EDTA 1 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

NMRFAM-SPARKY - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE NEO 800 MHz

Related Database Links:

UNP Q9H9Q4

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