BMRB Entry 51756

Name: Oct4_aa1-145_tev
Published: 2023-01-05

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51756

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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_aa1-145_tev

Deposition date:

2023-01-02

Original release date:

2023-01-05

Authors:

Theillet, Francois-Xavier

Citation:

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:

Assembly members:
entity_1, polymer, 151 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: pET-41b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GMAGHLASDFAFSPPPGGGG DGPGGPEPGWVDPRTWLSFQ GPPGGPGIGPGVGPGSEVWG IPPCPPPYEFCGGMAYCGPQ VGVGLVPQGGLETSQPEGEA GVGVESNSDGASPEPCTVTP GAVKLEKEKLEQNPEESQDI KALQKENLYFQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	379
15N chemical shifts	120
1H chemical shifts	120

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Oct4_aa1-145_tev	1

Entities:

Entity 1, Oct4_aa1-145_tev 151 residues - Formula weight is not available

1

GLY

MET

ALA

GLY

HIS

LEU

ALA

SER

ASP

PHE

2

ALA

PHE

SER

PRO

GLY

3

ASP

GLY

PRO

GLY

PRO

GLU

PRO

GLY

TRP

4

VAL

ASP

PRO

ARG

THR

TRP

LEU

SER

PHE

GLN

5

GLY

PRO

GLY

PRO

GLY

ILE

GLY

PRO

6

GLY

VAL

GLY

PRO

GLY

SER

GLU

VAL

TRP

GLY

7

ILE

PRO

CYS

PRO

TYR

GLU

PHE

8

CYS

GLY

MET

ALA

TYR

CYS

GLY

PRO

GLN

9

VAL

GLY

VAL

GLY

LEU

VAL

PRO

GLN

GLY

10

LEU

GLU

THR

SER

GLN

PRO

GLU

GLY

GLU

ALA

11

GLY

VAL

GLY

VAL

GLU

SER

ASN

SER

ASP

GLY

12

ALA

SER

PRO

GLU

PRO

CYS

THR

VAL

THR

PRO

13

GLY

ALA

VAL

LYS

LEU

GLU

LYS

GLU

LYS

LEU

14

GLU

GLN

ASN

PRO

GLU

SER

GLN

ASP

ILE

15

LYS

ALA

LEU

GLN

LYS

GLU

ASN

LEU

TYR

PHE

16

GLN

Samples:

sample_1: entity_1, [U-98% 13C; U-98% 15N], 600 ± 100 uM; HEPES 10 mM; sodium chloride 50 mM; ethanol 1%; PMSF 1 mM; TCEP 4 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 600 MHz

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