BMRB Entry 51758

Name: Oct4_aa286-360_tev
Published: 2023-01-05

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51758

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

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Title: Oct4_aa286-360_tev

Deposition date: 2023-01-03 Original release date: 2023-01-05

Authors: Theillet, Francois-Xavier

Citation: Theillet, Francois-Xavier. "Structural characterization of Oct4, Sox2, Nanog and Esrrb disordered domains, and a method to identify their phospho-dependent binding partners." C. R. Chim. ., .-..

Assembly members:
entity_1, polymer, 82 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: pET-41b(+)

Entity Sequences (FASTA):
entity_1: GKRSSSDYAQREDFEAAGSP FSGGPVSFPLAPGPHFGTPG YGSPHFTALYSSVPFPEGEA FPPVSVTTLGSPMHSNENLY FQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	228
15N chemical shifts	68
1H chemical shifts	68

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Oct4_aa286-360-tev	1

Entities:

Entity 1, Oct4_aa286-360-tev 82 residues - Formula weight is not available

1

GLY

LYS

ARG

SER

ASP

TYR

ALA

GLN

2

ARG

GLU

ASP

PHE

GLU

ALA

GLY

SER

PRO

3

PHE

SER

GLY

PRO

VAL

SER

PHE

PRO

LEU

4

ALA

PRO

GLY

PRO

HIS

PHE

GLY

THR

PRO

GLY

5

TYR

GLY

SER

PRO

HIS

PHE

THR

ALA

LEU

TYR

6

SER

VAL

PRO

PHE

PRO

GLU

GLY

GLU

ALA

7

PHE

PRO

VAL

SER

VAL

THR

LEU

GLY

8

SER

PRO

MET

HIS

SER

ASN

GLU

ASN

LEU

TYR

9

PHE

GLN

Samples:

sample_1: entity_1, [U-98% 13C; U-98% 15N], 500 ± 100 uM; HEPES 10 mM; sodium chloride 50 mM; DSS 0.1 mM

sample_conditions_1: ionic strength: 0.06 M; pH: 6.8; pressure: 1 atm; temperature: 283 K

Experiments:

Name	Sample	Sample state	Sample conditions
1D 1H	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D H(NCA)NH	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR v2.1 - chemical shift assignment

TOPSPIN v3 - collection, processing

NMR spectrometers:

Bruker AVANCE III 700 MHz

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