BMRB Entry 34152

Name: Solution NMR structure of DREB2A(255-272) bound to RCD1-RST
Published: 2018-04-13

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PDB ID: 5oap
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34152
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR structure of DREB2A(255-272) bound to RCD1-RST

Deposition date:

2017-06-23

Original release date:

2018-04-13

Authors:

Bugge, K.; Staby, L.; Skriver, K.; Kragelund, B.

Citation:

Citation: Bugge, Katrine; Staby, Lasse; Kemplen, Katherine; O'Shea, Charlotte; Bendsen, Sidsel; Jensen, Mikael; Olsen, Johan; Skriver, Karen; Kragelund, Birthe. "Structure of Radical-Induced Cell Death1 Hub Domain Reveals a Common aa-Scaffold for Disorder in Transcriptional Networks" Structure 26, 734-746 (2018).
PubMed: 29657132

Assembly members:

Assembly members:
DREB2A, polymer, 18 residues, 2057.134 Da.

Natural source:

Natural source: Common Name: Thale cress Taxonomy ID: 3702 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Arabidopsis thaliana

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
DREB2A: SSDMFDVDELLRDLNGDD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	49
15N chemical shifts	15
1H chemical shifts	95

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 18 residues - 2057.134 Da.

1

SER

ASP

MET

PHE

ASP

VAL

ASP

GLU

LEU

2

LEU

ARG

ASP

LEU

ASN

GLY

ASP

Samples:

sample_1: DREB2A, [U-13C; U-15N], 240 uM; DSS 0.7 mM; RCD1-RST 240 uM; sodium azide 0.2 mg/mL; sodium chloride 100 mM

sample_2: DREB2A, [U-15N], 200 uM; DSS 0.7 mM; RCD1-RST 200 uM; sodium azide 0.2 mg/mL; sodium chloride 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNHA	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

Analysis, CCPN - chemical shift assignment, data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

ProcheckNMR, Laskowski and MacArthur - geometry optimization

TALOS, Cornilescu, Delaglio and Bax - data analysis

TOPSPIN, Bruker Biospin - collection

VNMR, Varian - collection

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

Varian INOVA 800 MHz
Bruker Avance 750 MHz
Bruker Avance 600 MHz
Varian INOVA 750 MHz

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