BMRB Entry 50603

Name: Human Glucocorticoid Receptor DNA binding domain (DBD) assigned chemical shifts
Published: 2021-05-07

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50603

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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:

Human Glucocorticoid Receptor DNA binding domain (DBD) assigned chemical shifts

Deposition date:

2020-11-30

Original release date:

2021-05-07

Authors:

Grasso, Emily; Majumdar, Ananya; Wrabl, James; Frueh, Dominique; Hilser, Vincent

Citation:

Citation: Grasso, Emily; Majumdar, Ananya; Wrabl, James; Frueh, Dominique; Hilser, Vincent. "Conserved allosteric ensembles in a disordered protein using TROSY/Anti-TROSY R 2-filtered spectroscopy" Biophys. J. 120, 2498-2510 (2021).
PubMed: 33901472

Assembly members:

Assembly members:
entity_1, polymer, 87 residues, Formula weight is not available
entity_ZN, non-polymer, 65.409 Da.

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: pj411

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSGSWLCLVCSDEASGCHYG VLTCGSCKVFFKRAVEGQHN YLCAGRNDCIIDKIRRKNCP ACRYRKCLQAGMNLEARKTK KKIKGIQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	238
15N chemical shifts	82
1H chemical shifts	82

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	protein	1
2	zinc 1	2
3	zinc 2	2

Entities:

Entity 1, protein 87 residues - Formula weight is not available

The initial 5 amino acids remain after thrombin cleavage; residue 420 is the initial L in the sequence.

1

GLY

SER

GLY

SER

TRP

LEU

CYS

LEU

VAL

CYS

2

SER

ASP

GLU

ALA

SER

GLY

CYS

HIS

TYR

GLY

3

VAL

LEU

THR

CYS

GLY

SER

CYS

LYS

VAL

PHE

4

PHE

LYS

ARG

ALA

VAL

GLU

GLY

GLN

HIS

ASN

5

TYR

LEU

CYS

ALA

GLY

ARG

ASN

ASP

CYS

ILE

6

ILE

ASP

LYS

ILE

ARG

LYS

ASN

CYS

PRO

7

ALA

CYS

ARG

TYR

ARG

LYS

CYS

LEU

GLN

ALA

8

GLY

MET

ASN

LEU

GLU

ALA

ARG

LYS

THR

LYS

9

LYS

ILE

LYS

GLY

ILE

GLN

Entity 2, zinc 1 - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: DBD monomer, [U-13C; U-15N; U-2H], 165 uM; sodium chloride 100 mM; sodium phosphate 20 mM; TCEP 5 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 0.16 M; pH: 7.0; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

SPARKY - data analysis

TOPSPIN - collection

NMRPipe - processing

NMR spectrometers:

Bruker Avance 600 MHz

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