BMRB Entry 50742

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50742

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Title:
1H,13C,15N backbone resonance assignment for 1-164 construct of XRCC4
Deposition date:
2021-02-01
Original release date:
2021-06-28
Authors:
Cabello-Lobato, Maria Jose; Schmidt, Christine; Cliff, Matthew
Citation:

Citation: Cabello-Lobato, Maria Jose; Schmidt, Christine; Cliff, Matthew. "1H, 13C, 15N backbone resonance assignment for the 1-164 construct of human XRCC4"  Biomol. NMR Assignments 15, 389-395 (2021).
PubMed: 34173222

Assembly members:

Assembly members:
entity_1, polymer, 195 residues, 22158.71 Da.

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: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH MASENLYFQGSMERKISRIH LVSEPSITHFLQVSWEKTLE SGFVITLTDGHSAWTGTVSE SEISQEADDMAMEKGKYVGE LRKALLSGAGPADVYTFNFS KESAYFFFEKNLKDVSFRLG SFNLEKVENPAEVIRELIAY ALDTIAENQAKNEHLQKENE RLLRDWNDVQGRFEK

Data sets:
Data typeCount
13C chemical shifts517
15N chemical shifts172
1H chemical shifts172

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1XRCC4 Dimer, A1
2XRCC4 Dimer, B1

Entities:

Entity 1, XRCC4 Dimer, A 195 residues - 22158.71 Da.

Cys93 --> Ala; Cys128-->Ala; Cys130-->Ala. Stop codon @ 165

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METALASERGLUASNLEUTYRPHEGLNGLY
4   SERMETGLUARGLYSILESERARGILEHIS
5   LEUVALSERGLUPROSERILETHRHISPHE
6   LEUGLNVALSERTRPGLULYSTHRLEUGLU
7   SERGLYPHEVALILETHRLEUTHRASPGLY
8   HISSERALATRPTHRGLYTHRVALSERGLU
9   SERGLUILESERGLNGLUALAASPASPMET
10   ALAMETGLULYSGLYLYSTYRVALGLYGLU
11   LEUARGLYSALALEULEUSERGLYALAGLY
12   PROALAASPVALTYRTHRPHEASNPHESER
13   LYSGLUSERALATYRPHEPHEPHEGLULYS
14   ASNLEULYSASPVALSERPHEARGLEUGLY
15   SERPHEASNLEUGLULYSVALGLUASNPRO
16   ALAGLUVALILEARGGLULEUILEALATYR
17   ALALEUASPTHRILEALAGLUASNGLNALA
18   LYSASNGLUHISLEUGLNLYSGLUASNGLU
19   ARGLEULEUARGASPTRPASNASPVALGLN
20   GLYARGPHEGLULYS

Samples:

sample_1: XRCC4 Dimer, [U-100% 13C; U-100% 15N; U-80% 2H], 500 ± 100 uM; HEPES 20 ± 0.1 mM; sodium chloride 140 ± 0.1 mM; EDTA 1 ± 0.01 mM; DTT 2 ± 0.1 mM; Arginine 100 ± 0.1 mM; Glutamate 100 ± 0.1 mM; sodium azide 0.02 ± 0.0001 %; TSP, [U-80% 2H], 0.01 ± 0.0001 %

sample_conditions_1: ionic strength: 0.363 M; pH: 6.8; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.6 - collection, processing

ANALYSIS v2.4 - chemical shift assignment, data analysis, peak picking

TALOS+ - data analysis

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

Related Database Links:

UNP Q13426
AlphaFold Q9UP94

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