BMRB Entry 51964

Name: fl SOX2
Published: 2024-02-17

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51964

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

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

fl SOX2

Deposition date:

2023-05-16

Original release date:

2024-02-17

Authors:

Bjarnasson, Sveinn; Prestel, Andreas; Heidarsson, Petur

Citation:

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).
PubMed: 38365983

Assembly members:

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

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: pet24b

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
heteronucl_NOEs
- heteronucl_NOEs_1
heteronucl_T1_relaxation
- heteronucl_T1_relaxation_1
heteronucl_T2_relaxation
- heteronucl_T2_relaxation_1

Data type	Count
13C chemical shifts	425
15N chemical shifts	285
1H chemical shifts	285
T1 relaxation values	214
T2 relaxation values	214
heteronuclear NOE values	214

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	fl SOX2	1

Entities:

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

1

MET

TYR

ASN

MET

GLU

THR

GLU

LEU

LYS

2

PRO

GLY

PRO

GLN

THR

SER

GLY

3

GLY

ASN

SER

THR

ALA

4

GLY

ASN

GLN

LYS

ASN

SER

PRO

ASP

ARG

5

VAL

LYS

ARG

PRO

MET

ASN

ALA

PHE

MET

VAL

6

TRP

SER

ARG

GLY

GLN

ARG

LYS

MET

ALA

7

GLN

GLU

ASN

PRO

LYS

MET

HIS

ASN

SER

GLU

8

ILE

SER

LYS

ARG

LEU

GLY

ALA

GLU

TRP

LYS

9

LEU

SER

GLU

THR

GLU

LYS

ARG

PRO

PHE

10

ILE

ASP

GLU

ALA

LYS

ARG

LEU

ARG

ALA

LEU

11

HIS

MET

LYS

GLU

HIS

PRO

ASP

TYR

LYS

TYR

12

ARG

PRO

ARG

LYS

THR

LYS

THR

LEU

MET

13

LYS

ASP

LYS

TYR

THR

LEU

PRO

GLY

14

LEU

ALA

PRO

GLY

ASN

SER

MET

ALA

15

SER

GLY

VAL

GLY

VAL

GLY

ALA

GLY

LEU

GLY

16

ALA

GLY

VAL

ASN

GLN

ARG

MET

ASP

SER

TYR

17

ALA

HIS

MET

ASN

GLY

TRP

SER

ASN

GLY

SER

18

TYR

SER

MET

GLN

ASP

GLN

LEU

GLY

TYR

19

PRO

GLN

HIS

PRO

GLY

LEU

ASN

ALA

HIS

GLY

20

ALA

GLN

MET

GLN

PRO

MET

HIS

ARG

TYR

21

ASP

VAL

SER

ALA

LEU

GLN

TYR

ASN

SER

MET

22

THR

SER

GLN

THR

TYR

MET

ASN

GLY

SER

23

PRO

THR

TYR

SER

MET

SER

TYR

SER

GLN

24

GLY

THR

PRO

GLY

MET

ALA

LEU

GLY

SER

MET

25

GLY

SER

VAL

LYS

SER

GLU

ALA

SER

26

SER

PRO

VAL

THR

SER

HIS

27

SER

ARG

ALA

PRO

CYS

GLN

ALA

GLY

ASP

LEU

28

ARG

ASP

MET

ILE

SER

MET

TYR

LEU

PRO

GLY

29

ALA

GLU

VAL

PRO

GLU

PRO

ALA

PRO

SER

30

ARG

LEU

HIS

MET

SER

GLN

HIS

TYR

GLN

SER

31

GLY

PRO

VAL

PRO

GLY

THR

ALA

ILE

ASN

GLY

32

THR

LEU

PRO

LEU

SER

HIS

MET

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D (H)N(CA)NH	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
1H-15N heteronoe	sample_2	isotropic	sample_conditions_1
T2/R2 relaxation	sample_2	isotropic	sample_conditions_1
T1/R1 relaxation	sample_2	isotropic	sample_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 peaks
SPARKY: Backbone or all simulated peaks