BMRB Entry 53083

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53083

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

Title:
1H, 15N and 13C backbone resonance assignments of the nuclease domain (residues 2-349) of flap endonuclease from Plasmodium falciparum
Deposition date:
2025-04-28
Original release date:
2025-08-11
Authors:
do Aido-Machado, Rodolpho; Baxter, Nicola; Rowe, Michelle; Waltho, Jonathan
Citation:

Citation: do Aido-Machado, Rodolpho; Baxter, Nicola; Rowe, Michelle; Pohare, Manoj; Vitovski, Srdjan; Sayers, Jon; Waltho, Jonathan. "1H, 15N and 13C backbone resonance assignments of flap endonuclease from Plasmodium falciparum"  Biomol. NMR Assignments ., .-. (2025).
PubMed: 40781450

Assembly members:

Assembly members:
entity_1, polymer, 348 residues, 39635.59 Da.
entity_MG, non-polymer, 24.305 Da.

Natural source:

Natural source:   Common Name: Plasmodium falciparum   Taxonomy ID: 5833   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Plasmodium falciparum

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pTTQ18-T5

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GIKGLTKFIADAAPNAIKEI KIESLMGRIIAIDASMSLYQ FIIAIRDSEQYGNLTNESGE TTSHISGLMSRSIRLMENGL KPIYVFDGAPPELKGSELEK RGEKRQKAEELLKKAKEEGN LEEIKKQSGRTVRVTRKQNE EAKKLLTLMGIPIIEAPCEA ESQCAFLTKYNLAHATATED ADALVFGTKILIRNLNANAT SNQNKNKNNSKRGYILTEIN LEQVLKGLNLTMDEFIDFCI LCGCDYCDTIKGIGSKTAYN LIKEYNCIEKIIENIDQNKY QVPSNFRFQEARKSFINPNV LPKEDIKIDWNEPQIEELKH FLIKDYNFNELRVTNYINRL LKARKVTT

Data sets:
Data typeCount
13C chemical shifts931
15N chemical shifts298
1H chemical shifts298

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1fen, chain 11
2fen, chain 21
3Mg ion, 12
4Mg ion, 22

Entities:

Entity 1, fen, chain 1 348 residues - 39635.59 Da.

M1 is not present for the system under study

1   GLYILELYSGLYLEUTHRLYSPHEILEALA
2   ASPALAALAPROASNALAILELYSGLUILE
3   LYSILEGLUSERLEUMETGLYARGILEILE
4   ALAILEASPALASERMETSERLEUTYRGLN
5   PHEILEILEALAILEARGASPSERGLUGLN
6   TYRGLYASNLEUTHRASNGLUSERGLYGLU
7   THRTHRSERHISILESERGLYLEUMETSER
8   ARGSERILEARGLEUMETGLUASNGLYLEU
9   LYSPROILETYRVALPHEASPGLYALAPRO
10   PROGLULEULYSGLYSERGLULEUGLULYS
11   ARGGLYGLULYSARGGLNLYSALAGLUGLU
12   LEULEULYSLYSALALYSGLUGLUGLYASN
13   LEUGLUGLUILELYSLYSGLNSERGLYARG
14   THRVALARGVALTHRARGLYSGLNASNGLU
15   GLUALALYSLYSLEULEUTHRLEUMETGLY
16   ILEPROILEILEGLUALAPROCYSGLUALA
17   GLUSERGLNCYSALAPHELEUTHRLYSTYR
18   ASNLEUALAHISALATHRALATHRGLUASP
19   ALAASPALALEUVALPHEGLYTHRLYSILE
20   LEUILEARGASNLEUASNALAASNALATHR
21   SERASNGLNASNLYSASNLYSASNASNSER
22   LYSARGGLYTYRILELEUTHRGLUILEASN
23   LEUGLUGLNVALLEULYSGLYLEUASNLEU
24   THRMETASPGLUPHEILEASPPHECYSILE
25   LEUCYSGLYCYSASPTYRCYSASPTHRILE
26   LYSGLYILEGLYSERLYSTHRALATYRASN
27   LEUILELYSGLUTYRASNCYSILEGLULYS
28   ILEILEGLUASNILEASPGLNASNLYSTYR
29   GLNVALPROSERASNPHEARGPHEGLNGLU
30   ALAARGLYSSERPHEILEASNPROASNVAL
31   LEUPROLYSGLUASPILELYSILEASPTRP
32   ASNGLUPROGLNILEGLUGLULEULYSHIS
33   PHELEUILELYSASPTYRASNPHEASNGLU
34   LEUARGVALTHRASNTYRILEASNARGLEU
35   LEULYSALAARGLYSVALTHRTHR

Entity 2, Mg ion, 1 - Mg - 24.305 Da.

1   MG

Samples:

sample_1: fen_pf, [U-100% 13C; U-100% 15N; U-80% 2H], 0.75 mM; magnesium chloride 10.0 mM; sodium phosphate 20.0 mM; potassium chloride 30.0 mM; EDTA 0.1 mM; sodium azide 2.0 mM; TCEP 2.0 mM; TSP, [U-100% 2H], 1.0 mM; D2O, [U-100% 2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 0.111 M; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1D 1Hsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D TROSY-HNCAsample_1isotropicsample_conditions_1
3D TROSY-HN(CO)CAsample_1isotropicsample_conditions_1
3D TROSY-HN(CA)COsample_1isotropicsample_conditions_1
3D TROSY-HNCOsample_1isotropicsample_conditions_1
3D TROSY-HNCACBsample_1isotropicsample_conditions_1
3D TROSY-HN(CO)CACBsample_1isotropicsample_conditions_1
3D TROSY-(H)N(COCA)NNHsample_1isotropicsample_conditions_1
3D TROSY-H(NCOCA)NNHsample_1isotropicsample_conditions_1

Software:

TOPSPIN v4.0.5 - collection, processing

Felix - chemical shift assignment, peak picking

TALOS-N - data analysis

NMR spectrometers:

  • Bruker AVANCE NEO 800 MHz

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