BMRB Entry 26350

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26350

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Title:
Backbone 1H and 15N Chemical Shift Assignments for FOXO3a (1-284) phosphorylated on T32 and S253
Deposition date:
2024-08-30
Original release date:
2025-09-15
Authors:
Enomoto, Shota; Nakatsuka, Shoichi; Kuwayama, Tomoya; Kawatsu, Kosaku; Yokogawa, Mariko; Osawa, Masanori
Citation:

Citation: Enomoto, Shota; Nakatsuka, Shoichi; Kuwayama, Tomoya; Kawatsu, Kosaku; Yokogawa, Mariko; Osawa, Masanori. "NMR (1)H, (13)C, (15)N backbone resonance assignments of 14-3-3z binding region of human FOXO3a (residues 1-284)."  Biomol. NMR Assign. 18, 275-283 (2024).
PubMed: 39259470

Assembly members:

Assembly members:
FOXO3a (1-284) phosphorylated on T32 and S253, polymer, 289 residues, 30390 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: pGEX6P-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FOXO3a (1-284) phosphorylated on T32 and S253: GPLGSMAEAPASPAPLSPLE VELDPEFEPQSRPRSCXWPL QRPELQASPAKPSGETAADS MIPEEEDDEDDEDGGGRAGS AMAIGGGGGSGTLGSGLLLE DSARVLAPGGQDPGSGPATA AGGLSGGTQALLQPQQPLPP PQPGAAGGSGQPRKCSSRRN AWGNLSYADLITRAIESSPD KRLTLSQIYEWMVRCVPYFK DKGDSNSSAGWKNSIRHNLS LHSRFMRVQNEGTGKSSWWI INPDGGKSGKAPRRRAVXMD NSNKYTKSRGRAAKKKAALQ TAPESADDS

Data sets:
Data typeCount
15N chemical shifts212
1H chemical shifts212

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1subunit 11

Entities:

Entity 1, subunit 1 289 residues - 30390 Da.

1   GLYPROLEUGLYSERMETALAGLUALAPRO
2   ALASERPROALAPROLEUSERPROLEUGLU
3   VALGLULEUASPPROGLUPHEGLUPROGLN
4   SERARGPROARGSERCYSTPOTRPPROLEU
5   GLNARGPROGLULEUGLNALASERPROALA
6   LYSPROSERGLYGLUTHRALAALAASPSER
7   METILEPROGLUGLUGLUASPASPGLUASP
8   ASPGLUASPGLYGLYGLYARGALAGLYSER
9   ALAMETALAILEGLYGLYGLYGLYGLYSER
10   GLYTHRLEUGLYSERGLYLEULEULEUGLU
11   ASPSERALAARGVALLEUALAPROGLYGLY
12   GLNASPPROGLYSERGLYPROALATHRALA
13   ALAGLYGLYLEUSERGLYGLYTHRGLNALA
14   LEULEUGLNPROGLNGLNPROLEUPROPRO
15   PROGLNPROGLYALAALAGLYGLYSERGLY
16   GLNPROARGLYSCYSSERSERARGARGASN
17   ALATRPGLYASNLEUSERTYRALAASPLEU
18   ILETHRARGALAILEGLUSERSERPROASP
19   LYSARGLEUTHRLEUSERGLNILETYRGLU
20   TRPMETVALARGCYSVALPROTYRPHELYS
21   ASPLYSGLYASPSERASNSERSERALAGLY
22   TRPLYSASNSERILEARGHISASNLEUSER
23   LEUHISSERARGPHEMETARGVALGLNASN
24   GLUGLYTHRGLYLYSSERSERTRPTRPILE
25   ILEASNPROASPGLYGLYLYSSERGLYLYS
26   ALAPROARGARGARGALAVALSEPMETASP
27   ASNSERASNLYSTYRTHRLYSSERARGGLY
28   ARGALAALALYSLYSLYSALAALALEUGLN
29   THRALAPROGLUSERALAASPASPSER

Samples:

sample_1: FOXO3a (1-284) phosphorylated on T32 and S253, [U-15N; U-2H], 97 uM; DTT 1 mM; sodium chloride 100 mM; sodium phosphate 20 mM; H2O 90%; D2O, [U-2H], 10%

sample_2: FOXO3a (1-284) phosphorylated on T32 and S253, [U-15N; U-2H], 169 uM; DTT 1 mM; sodium chloride 100 mM; sodium phosphate 20 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: pH: 6.4; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

SPARKY v3.190 - chemical shift assignment

TOPSPIN v4.2.0 - processing

NMR spectrometers:

  • Bruker AVANCE NEO 600 MHz
  • Bruker AVANCE III 800 MHz

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