BMRB Entry 51717

Name: Esrrb_aa1-102
Published: 2022-12-06

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51717

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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: Esrrb_aa1-102

Deposition date: 2022-12-01 Original release date: 2022-12-06

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. ., .-. (2023).

Assembly members:
entity_1, polymer, 103 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: GMSSEDRHLGSSAGSFIKTE PSSPSSGIDALSHHSPSGSS DASGGFGIALSTHANGLDSP PMFAGAGLGGNPARKSYEDC TSGIMEDSAIKAEYMLNAIP KRL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	280
15N chemical shifts	93
1H chemical shifts	93

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Esrrb_aa1-102_C12A-C72A-C91A	1

Entities:

Entity 1, Esrrb_aa1-102_C12A-C72A-C91A 103 residues - Formula weight is not available

1

GLY

MET

SER

GLU

ASP

ARG

HIS

LEU

GLY

2

SER

ALA

GLY

SER

PHE

ILE

LYS

THR

GLU

3

PRO

SER

PRO

SER

GLY

ILE

ASP

ALA

4

LEU

SER

HIS

SER

PRO

SER

GLY

SER

5

ASP

ALA

SER

GLY

PHE

GLY

ILE

ALA

LEU

6

SER

THR

HIS

ALA

ASN

GLY

LEU

ASP

SER

PRO

7

PRO

MET

PHE

ALA

GLY

ALA

GLY

LEU

GLY

8

ASN

PRO

ALA

ARG

LYS

SER

TYR

GLU

ASP

CYS

9

THR

SER

GLY

ILE

MET

GLU

ASP

SER

ALA

ILE

10

LYS

ALA

GLU

TYR

MET

LEU

ASN

ALA

ILE

PRO

11

LYS

ARG

LEU

Samples:

sample_1: Esrrb_aa1-102_C12A-C72A-C91A, [U-98% 15N], 900 ± 100 uM; TCEP 2 mM; HEPES 10 mM; sodium chloride 50 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)N(CA)NH	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR v2.1 - chemical shift assignment

TOPSPIN v3 - acquisition, 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