BMRB Entry 4153

Name: High-Resolution Solution Structure of the Retinoid X Receptor DNA-Binding Domain
Published: 2000-06-30

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PDB ID: 1rxr
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4153
MolProbity Validation Chart

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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:

High-Resolution Solution Structure of the Retinoid X Receptor DNA-Binding Domain

Deposition date:

1998-06-24

Original release date:

2000-06-30

Authors:

Holmbeck, Signe; Foster, M.; Casimiro, D.; Sem, D.; Dyson, H.; Wright, Peter

Citation:

Citation: Holmbeck, Signe; Foster, M.; Casimiro, D.; Sem, D.; Dyson, H.; Wright, Peter. "High-Resolution Solution Structure of the Retinoid X Receptor DNA-Binding Domain" J. Mol. Biol. 281, 271-284 (1998).

Assembly members:

Assembly members:
RXR-alpha, polymer, 83 residues, Formula weight is not available
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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RXR-alpha: FTKHICAICGDRSSGKHYGV YSCEGCKGFFKRTVRKDLTY TCRDNKDCLIDKRQRNRCQY CRYQKALAMGMKREAVQEER QRX

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_one

Data type	Count
13C chemical shifts	254
15N chemical shifts	84
1H chemical shifts	525

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RXR-DBD	1
2	Zn 1	2
3	Zn 2	2

Entities:

Entity 1, RXR-DBD 83 residues - Formula weight is not available

1

PHE

THR

LYS

HIS

ILE

CYS

ALA

ILE

CYS

GLY

2

ASP

ARG

SER

GLY

LYS

HIS

TYR

GLY

VAL

3

TYR

SER

CYS

GLU

GLY

CYS

LYS

GLY

PHE

4

LYS

ARG

THR

VAL

ARG

LYS

ASP

LEU

THR

TYR

5

THR

CYS

ARG

ASP

ASN

LYS

ASP

CYS

LEU

ILE

6

ASP

LYS

ARG

GLN

ARG

ASN

ARG

CYS

GLN

TYR

7

CYS

ARG

TYR

GLN

LYS

ALA

LEU

ALA

MET

GLY

8

MET

LYS

ARG

GLU

ALA

VAL

GLN

GLU

ARG

9

GLN

ARG

NVA

Entity 2, Zn 1 - Zn - 65.409 Da.

1

ZN

Samples:

sample_one: RXR-alpha 1.7 mM

sample_conditions_one: ionic strength: 0.12 M; pH: 6.6; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
CBCA(CO)NH	sample_one	not available	sample_conditions_one
HBHA(CBCACO)NH	sample_one	not available	sample_conditions_one
CBCANH	sample_one	not available	sample_conditions_one
C(CO)NH-TOCSY	sample_one	not available	sample_conditions_one
HCCH-COSY	sample_one	not available	sample_conditions_one
HCCH-TOCSY	sample_one	not available	sample_conditions_one
13C-EDITED NOESY	sample_one	not available	sample_conditions_one
15N-EDITED NOESY	sample_one	not available	sample_conditions_one
15N-EDITED TOCSY	sample_one	not available	sample_conditions_one
HNHA	sample_one	not available	sample_conditions_one
HNHB	sample_one	not available	sample_conditions_one
HACAHB-COSY	sample_one	not available	sample_conditions_one
13C-13CO	sample_one	not available	sample_conditions_one
13C-15N SPIN ECHO DIFFERENCE CT-HSQC	sample_one	not available	sample_conditions_one

Software:

No software information available

NMR spectrometers:

Bruker AMX 500 MHz
Bruker DMX 600 MHz

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