BMRB Entry 51780

Name: Nanog_aa1-85
Published: 2023-01-18

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51780

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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: Nanog_aa1-85

Deposition date: 2023-01-10 Original release date: 2023-01-18

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, 86 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: pet41b(+)

Entity Sequences (FASTA):
entity_1: GMSVDPACPQSLPCFEASDC KESSPMPVICGPEENYPSLQ MSSAEMPHTETVSPLPSSMD LLIQDSPDSSTSPKGKQPTS AEKSVA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	239
15N chemical shifts	72
1H chemical shifts	72

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Nanog aa1-85	1

Entities:

Entity 1, Nanog aa1-85 86 residues - Formula weight is not available

One supplementary Glycine in N-terminal, remaining from Tev-motif (ENLYFQG) after cleavage by Tev-protease.

1

GLY

MET

SER

VAL

ASP

PRO

ALA

CYS

PRO

GLN

2

SER

LEU

PRO

CYS

PHE

GLU

ALA

SER

ASP

CYS

3

LYS

GLU

SER

PRO

MET

PRO

VAL

ILE

CYS

4

GLY

PRO

GLU

ASN

TYR

PRO

SER

LEU

GLN

5

MET

SER

ALA

GLU

MET

PRO

HIS

THR

GLU

6

THR

VAL

SER

PRO

LEU

PRO

SER

MET

ASP

7

LEU

ILE

GLN

ASP

SER

PRO

ASP

SER

8

THR

SER

PRO

LYS

GLY

LYS

GLN

PRO

THR

SER

9

ALA

GLU

LYS

SER

VAL

ALA

Samples:

sample_1: Nanog_aa1-85, [U-98% 13C; U-98% 15N], 450 ± 100 uM; DSS 0.1 mM; HEPES 20 mM; sodium chloride 50 mM; TCEP 5 mM; cocktail protease inhibitors 2 tablet/100mL

sample_conditions_1: ionic strength: 70 mM; pH: 6.5; 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:

TOPSPIN v3 - collection, processing

CcpNMR v2.1 - chemical shift assignment

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