BMRB Entry 26757

Name: 1H, 13C, 15N backbone and 1H, 13C methionine methyl chemical shifts of human F602S Glucocorticoid receptor Ligand Binding Domain
Published: 2018-06-27

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR26757

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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:

1H, 13C, 15N backbone and 1H, 13C methionine methyl chemical shifts of human F602S Glucocorticoid receptor Ligand Binding Domain

Deposition date:

2016-03-11

Original release date:

2018-06-27

Authors:

Kohler, Christian; Weininger, Ulrich; Backstrom, Stefan; Carlstrom, Goran; Lepisto, Matti; Papavoine, Tineke; Edman, Karl; Akke, Mikael

Citation:

Citation: Kohler, Christian; Carlstrom, Goran; Tangefjord, Stefan; Papavoine, Tineke; Lepisto, Matti; Edman, Karl; Akke, Mikael. "Backbone 1H, 13C, and 15N resonance assignments of the ligand binding domain of the human wildtype glucocorticoid receptor and the F602S mutant variant" Biomol. NMR Assign. 12, 263-268 (2018).
PubMed: 29667121

Assembly members:

Assembly members:
Glucocorticoid_Receptor_Ligand_Binding_Domain, polymer, 250 residues, 29018.8 Da.
TIF-2_Nuclear_coactivator_2, polymer, 14 residues, 1705.9 Da.
entity_DEX, non-polymer, 392.461 Da.
entity_CPS, non-polymer, 614.877 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: pET24a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Glucocorticoid_Receptor_Ligand_Binding_Domain: GTPTLVSLLEVIEPEVLYAG YDSSVPDSYWRIMTTLNMLG GRQVIAAVKWAKAIPGFRNL HLDDQMTLLQYSWMSLMAFA LGWRSYRQSSANLLCFAPDL IINEQRMTLPCMYDQCKHML YVSSELHRLQVSYEEYLCMK TLLLLSSVPKDGLKSQELFD EIRMTYIKELGKAIVKREGN SSQNWQRFYQLTKLLDSMHE VVENLLNYCFQTFLDKTMSI EFPEMLAEIITNQIPKYSNG NIKKLLFHQK
TIF-2_Nuclear_coactivator_2: KENALLRYLLDKDD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	251
15N chemical shifts	231
1H chemical shifts	270

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Glucocorticoid Receptor Ligand Binding Domain	1
2	Dexamethasone	3
3	TIF-2 Nuclear coactivator 2	2
4	CHAPS	4

Entities:

Entity 1, Glucocorticoid Receptor Ligand Binding Domain 250 residues - 29018.8 Da.

First Gly remains from purification tag

1	GLY	THR	PRO	THR	LEU	VAL	SER	LEU	LEU	GLU
2	VAL	ILE	GLU	PRO	GLU	VAL	LEU	TYR	ALA	GLY
3	TYR	ASP	SER	SER	VAL	PRO	ASP	SER	TYR	TRP
4	ARG	ILE	MET	THR	THR	LEU	ASN	MET	LEU	GLY
5	GLY	ARG	GLN	VAL	ILE	ALA	ALA	VAL	LYS	TRP
6	ALA	LYS	ALA	ILE	PRO	GLY	PHE	ARG	ASN	LEU
7	HIS	LEU	ASP	ASP	GLN	MET	THR	LEU	LEU	GLN
8	TYR	SER	TRP	MET	SER	LEU	MET	ALA	PHE	ALA
9	LEU	GLY	TRP	ARG	SER	TYR	ARG	GLN	SER	SER
10	ALA	ASN	LEU	LEU	CYS	PHE	ALA	PRO	ASP	LEU
11	ILE	ILE	ASN	GLU	GLN	ARG	MET	THR	LEU	PRO
12	CYS	MET	TYR	ASP	GLN	CYS	LYS	HIS	MET	LEU
13	TYR	VAL	SER	SER	GLU	LEU	HIS	ARG	LEU	GLN
14	VAL	SER	TYR	GLU	GLU	TYR	LEU	CYS	MET	LYS
15	THR	LEU	LEU	LEU	LEU	SER	SER	VAL	PRO	LYS
16	ASP	GLY	LEU	LYS	SER	GLN	GLU	LEU	PHE	ASP
17	GLU	ILE	ARG	MET	THR	TYR	ILE	LYS	GLU	LEU
18	GLY	LYS	ALA	ILE	VAL	LYS	ARG	GLU	GLY	ASN
19	SER	SER	GLN	ASN	TRP	GLN	ARG	PHE	TYR	GLN
20	LEU	THR	LYS	LEU	LEU	ASP	SER	MET	HIS	GLU
21	VAL	VAL	GLU	ASN	LEU	LEU	ASN	TYR	CYS	PHE
22	GLN	THR	PHE	LEU	ASP	LYS	THR	MET	SER	ILE
23	GLU	PHE	PRO	GLU	MET	LEU	ALA	GLU	ILE	ILE
24	THR	ASN	GLN	ILE	PRO	LYS	TYR	SER	ASN	GLY
25	ASN	ILE	LYS	LYS	LEU	LEU	PHE	HIS	GLN	LYS

Entity 3, Dexamethasone - C22 H29 F O5 - 392.461 Da.

1

DEX

Entity 2, TIF-2 Nuclear coactivator 2 14 residues - 1705.9 Da.

Nuclear coactivator 2

1

LYS

GLU

ASN

ALA

LEU

ARG

TYR

LEU

2

ASP

LYS

ASP

Entity 4, CHAPS - C32 H58 N2 O7 S - 614.877 Da.

1

CPS

Samples:

sample_1: Glucocorticoid Receptor Ligand Binding Domain, [U-13C; U-15N; U-2H], 0.3 mM; Dexamethasone 50 uM; CHAPS 1%; TIF-2 Nuclear coactivator 2 0.3 mM; potassium phosphate 20 mM; DTT 2 mM; sodium azide 0.02%

sample_2: Glucocorticoid Receptor Ligand Binding Domain, L-methionine (methyl-13C), 0.3 mM; Dexamethasone 50 uM; CHAPS 1%; TIF-2 Nuclear coactivator 2 0.3 mM; potassium phosphate 20 mM; DTT 2 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 0.12 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
1H-15N TROSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

UNP	P04150
NCBI	NP_000167.1
AlphaFold	Q6N0A4

1	GLY	THR	PRO	THR	LEU	VAL	SER	LEU	LEU	GLU
2	VAL	ILE	GLU	PRO	GLU	VAL	LEU	TYR	ALA	GLY
3	TYR	ASP	SER	SER	VAL	PRO	ASP	SER	TYR	TRP
4	ARG	ILE	MET	THR	THR	LEU	ASN	MET	LEU	GLY
5	GLY	ARG	GLN	VAL	ILE	ALA	ALA	VAL	LYS	TRP
6	ALA	LYS	ALA	ILE	PRO	GLY	PHE	ARG	ASN	LEU
7	HIS	LEU	ASP	ASP	GLN	MET	THR	LEU	LEU	GLN
8	TYR	SER	TRP	MET	SER	LEU	MET	ALA	PHE	ALA
9	LEU	GLY	TRP	ARG	SER	TYR	ARG	GLN	SER	SER
10	ALA	ASN	LEU	LEU	CYS	PHE	ALA	PRO	ASP	LEU
11	ILE	ILE	ASN	GLU	GLN	ARG	MET	THR	LEU	PRO
12	CYS	MET	TYR	ASP	GLN	CYS	LYS	HIS	MET	LEU
13	TYR	VAL	SER	SER	GLU	LEU	HIS	ARG	LEU	GLN
14	VAL	SER	TYR	GLU	GLU	TYR	LEU	CYS	MET	LYS
15	THR	LEU	LEU	LEU	LEU	SER	SER	VAL	PRO	LYS
16	ASP	GLY	LEU	LYS	SER	GLN	GLU	LEU	PHE	ASP
17	GLU	ILE	ARG	MET	THR	TYR	ILE	LYS	GLU	LEU
18	GLY	LYS	ALA	ILE	VAL	LYS	ARG	GLU	GLY	ASN
19	SER	SER	GLN	ASN	TRP	GLN	ARG	PHE	TYR	GLN
20	LEU	THR	LYS	LEU	LEU	ASP	SER	MET	HIS	GLU
21	VAL	VAL	GLU	ASN	LEU	LEU	ASN	TYR	CYS	PHE
22	GLN	THR	PHE	LEU	ASP	LYS	THR	MET	SER	ILE
23	GLU	PHE	PRO	GLU	MET	LEU	ALA	GLU	ILE	ILE
24	THR	ASN	GLN	ILE	PRO	LYS	TYR	SER	ASN	GLY
25	ASN	ILE	LYS	LYS	LEU	LEU	PHE	HIS	GLN	LYS

1	GLY	THR	PRO	THR	LEU	VAL	SER	LEU	LEU	GLU
2	VAL	ILE	GLU	PRO	GLU	VAL	LEU	TYR	ALA	GLY
3	TYR	ASP	SER	SER	VAL	PRO	ASP	SER	TYR	TRP
4	ARG	ILE	MET	THR	THR	LEU	ASN	MET	LEU	GLY
5	GLY	ARG	GLN	VAL	ILE	ALA	ALA	VAL	LYS	TRP
6	ALA	LYS	ALA	ILE	PRO	GLY	PHE	ARG	ASN	LEU
7	HIS	LEU	ASP	ASP	GLN	MET	THR	LEU	LEU	GLN
8	TYR	SER	TRP	MET	SER	LEU	MET	ALA	PHE	ALA
9	LEU	GLY	TRP	ARG	SER	TYR	ARG	GLN	SER	SER
10	ALA	ASN	LEU	LEU	CYS	PHE	ALA	PRO	ASP	LEU
11	ILE	ILE	ASN	GLU	GLN	ARG	MET	THR	LEU	PRO
12	CYS	MET	TYR	ASP	GLN	CYS	LYS	HIS	MET	LEU
13	TYR	VAL	SER	SER	GLU	LEU	HIS	ARG	LEU	GLN
14	VAL	SER	TYR	GLU	GLU	TYR	LEU	CYS	MET	LYS
15	THR	LEU	LEU	LEU	LEU	SER	SER	VAL	PRO	LYS
16	ASP	GLY	LEU	LYS	SER	GLN	GLU	LEU	PHE	ASP
17	GLU	ILE	ARG	MET	THR	TYR	ILE	LYS	GLU	LEU
18	GLY	LYS	ALA	ILE	VAL	LYS	ARG	GLU	GLY	ASN
19	SER	SER	GLN	ASN	TRP	GLN	ARG	PHE	TYR	GLN
20	LEU	THR	LYS	LEU	LEU	ASP	SER	MET	HIS	GLU
21	VAL	VAL	GLU	ASN	LEU	LEU	ASN	TYR	CYS	PHE
22	GLN	THR	PHE	LEU	ASP	LYS	THR	MET	SER	ILE
23	GLU	PHE	PRO	GLU	MET	LEU	ALA	GLU	ILE	ILE
24	THR	ASN	GLN	ILE	PRO	LYS	TYR	SER	ASN	GLY
25	ASN	ILE	LYS	LYS	LEU	LEU	PHE	HIS	GLN	LYS