BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 51964

Title: fl SOX2   PubMed: 38365983

Deposition date: 2023-05-16 Original release date: 2024-02-17

Authors: Bjarnasson, Sveinn; Prestel, Andreas; Heidarsson, Petur

Citation: Bjarnason, Sveinn; McIvor, Jordan; Prestel, Andreas; Demeny, Kinga; Bullerjahn, Jakob; Kragelund, Birthe; Mercadante, Davide; Heidarsson, Petur. "DNA binding redistributes activation domain ensemble and accessibility in pioneer factor Sox2"  Nat. Commun. 15, 1445-1445 (2024).

Assembly members:
entity_1, polymer, 317 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet24b

Entity Sequences (FASTA):
entity_1: MYNMMETELKPPGPQQTSGG GGGNSTAAAAGGNQKNSPDR VKRPMNAFMVWSRGQRRKMA QENPKMHNSEISKRLGAEWK LLSETEKRPFIDEAKRLRAL HMKEHPDYKYRPRRKTKTLM KKDKYTLPGGLLAPGGNSMA SGVGVGAGLGAGVNQRMDSY AHMNGWSNGSYSMMQDQLGY PQHPGLNAHGAAQMQPMHRY DVSALQYNSMTSSQTYMNGS PTYSMSYSQQGTPGMALGSM GSVVKSEASSSPPVVTSSSH SRAPCQAGDLRDMISMYLPG AEVPEPAAPSRLHMSQHYQS GPVPGTAINGTLPLSHM

Data sets:
Data typeCount
13C chemical shifts425
15N chemical shifts285
1H chemical shifts285
T1 relaxation values214
T2 relaxation values214
heteronuclear NOE values214

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1fl SOX21

Entities:

Entity 1, fl SOX2 317 residues - Formula weight is not available

1   METTYRASNMETMETGLUTHRGLULEULYS
2   PROPROGLYPROGLNGLNTHRSERGLYGLY
3   GLYGLYGLYASNSERTHRALAALAALAALA
4   GLYGLYASNGLNLYSASNSERPROASPARG
5   VALLYSARGPROMETASNALAPHEMETVAL
6   TRPSERARGGLYGLNARGARGLYSMETALA
7   GLNGLUASNPROLYSMETHISASNSERGLU
8   ILESERLYSARGLEUGLYALAGLUTRPLYS
9   LEULEUSERGLUTHRGLULYSARGPROPHE
10   ILEASPGLUALALYSARGLEUARGALALEU
11   HISMETLYSGLUHISPROASPTYRLYSTYR
12   ARGPROARGARGLYSTHRLYSTHRLEUMET
13   LYSLYSASPLYSTYRTHRLEUPROGLYGLY
14   LEULEUALAPROGLYGLYASNSERMETALA
15   SERGLYVALGLYVALGLYALAGLYLEUGLY
16   ALAGLYVALASNGLNARGMETASPSERTYR
17   ALAHISMETASNGLYTRPSERASNGLYSER
18   TYRSERMETMETGLNASPGLNLEUGLYTYR
19   PROGLNHISPROGLYLEUASNALAHISGLY
20   ALAALAGLNMETGLNPROMETHISARGTYR
21   ASPVALSERALALEUGLNTYRASNSERMET
22   THRSERSERGLNTHRTYRMETASNGLYSER
23   PROTHRTYRSERMETSERTYRSERGLNGLN
24   GLYTHRPROGLYMETALALEUGLYSERMET
25   GLYSERVALVALLYSSERGLUALASERSER
26   SERPROPROVALVALTHRSERSERSERHIS
27   SERARGALAPROCYSGLNALAGLYASPLEU
28   ARGASPMETILESERMETTYRLEUPROGLY
29   ALAGLUVALPROGLUPROALAALAPROSER
30   ARGLEUHISMETSERGLNHISTYRGLNSER
31   GLYPROVALPROGLYTHRALAILEASNGLY
32   THRLEUPROLEUSERHISMET

Samples:

sample_1: fl SOX2, [U-100% 13C; U-100% 15N], 110 uM; DTT 5 mM; DSS 125 uM; sodium chloride 50 mM; sodium phosphate 20 mM

sample_2: fl SOX2, [U-100% 15N], 30 uM; DTT 5 mM; DSS 125 uM; sodium chloride 50 mM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 90 mM; pH: 5.5; pressure: 1 atm; temperature: 288.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D (H)N(CA)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
1H-15N heteronoesample_2isotropicsample_conditions_1
T2/R2 relaxationsample_2isotropicsample_conditions_1
T1/R1 relaxationsample_2isotropicsample_conditions_1

Software:

NMRPipe - processing

CcpNMR v2.5 - chemical shift assignment

qMDD - processing

TOPSPIN - collection

NMR spectrometers:

  • Bruker Avance III HD 750 MHz

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