BMRB Entry 53001

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53001

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Title:
Rad52 C-terminus 206-471
Deposition date:
2025-04-03
Original release date:
2025-11-14
Authors:
Ochsenbein, Francoise
Citation:

Citation: Ma, Emilie; Lakhal, Fadma; Litsardaki, Eleni; Ruault, Myriam; Audin, Maxime; Levrier, Natacha; Navarro, Emilie; Garnier, Mickael; Maloisel, Laurent; Depagne, Jordane; Brocas, Clementine; Thureau, Aurelien; Busso, Didier; Veaute, Xavier; Guerois, Raphael; Taddei, Angela; Ochsenbein, Francoise; Coic, Eric. "A large C-terminal Rad52 segment acts as a chaperone to Form and Stabilize Rad51 Filaments"  Nat. Commun. 16, 5589-5589 (2025).
PubMed: 40595518

Assembly members:

Assembly members:
entity_1, polymer, 266 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: petM30

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: KVTNTNPDSTKNLVKIENTV SRGTPMMAAPAEANSKNSSN KDTDLKSLDASKQDQDDLLD DSLMFSDDFQDDDLINMGNT NSNVLTTEKDPVVAKQSPTA SSNPEAEQITFVTAKAATSV QNERYIGEESIFDPKYQAQS IRHTVDQTTSKHVPASVLKD KTMTTARDSVYEKFAPKGKQ LSMKNNDKELGPHMLEGAGN QVPRETTPIKTNATAFPPAA APRFAPPSKVVHPNGNGAVP AVPQQRSTRREVGRPKINPL HARKPT

Data sets:
Data typeCount
13C chemical shifts739
15N chemical shifts245
1H chemical shifts241

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Rad52-206-4711

Entities:

Entity 1, Rad52-206-471 266 residues - Formula weight is not available

1   LYSVALTHRASNTHRASNPROASPSERTHR
2   LYSASNLEUVALLYSILEGLUASNTHRVAL
3   SERARGGLYTHRPROMETMETALAALAPRO
4   ALAGLUALAASNSERLYSASNSERSERASN
5   LYSASPTHRASPLEULYSSERLEUASPALA
6   SERLYSGLNASPGLNASPASPLEULEUASP
7   ASPSERLEUMETPHESERASPASPPHEGLN
8   ASPASPASPLEUILEASNMETGLYASNTHR
9   ASNSERASNVALLEUTHRTHRGLULYSASP
10   PROVALVALALALYSGLNSERPROTHRALA
11   SERSERASNPROGLUALAGLUGLNILETHR
12   PHEVALTHRALALYSALAALATHRSERVAL
13   GLNASNGLUARGTYRILEGLYGLUGLUSER
14   ILEPHEASPPROLYSTYRGLNALAGLNSER
15   ILEARGHISTHRVALASPGLNTHRTHRSER
16   LYSHISVALPROALASERVALLEULYSASP
17   LYSTHRMETTHRTHRALAARGASPSERVAL
18   TYRGLULYSPHEALAPROLYSGLYLYSGLN
19   LEUSERMETLYSASNASNASPLYSGLULEU
20   GLYPROHISMETLEUGLUGLYALAGLYASN
21   GLNVALPROARGGLUTHRTHRPROILELYS
22   THRASNALATHRALAPHEPROPROALAALA
23   ALAPROARGPHEALAPROPROSERLYSVAL
24   VALHISPROASNGLYASNGLYALAVALPRO
25   ALAVALPROGLNGLNARGSERTHRARGARG
26   GLUVALGLYARGPROLYSILEASNPROLEU
27   HISALAARGLYSPROTHR

Samples:

sample_1: Rad52 206-471, [U-100% 13C; U-100% 15N], 200 uM; sodium phosphate 20 mM; sodium chloride 150 mM; DTT 1 mM; EDTA 0.5 mM; AEBSF protease inhibitor 1 mM; D2O 5%; sodium azide 0.1%; DSS 0.1 uM

sample_conditions_1: ionic strength: 150 mM; pH: 7.4; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
sofast-HMQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CA)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

TOPSPIN v4.1.3 - collection, pro

SPARKY v3.114 - chemical shift assignment

NMR spectrometers:

  • Bruker DRX 700 MHz

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