BMRB Entry 30180

Name: N-terminal microdomain of 34-mers from HsDHODH - N-t(DH)
Published: 2017-09-11

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PDB ID: 5tce
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30180
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:

N-terminal microdomain of 34-mers from HsDHODH - N-t(DH)

Deposition date:

2016-09-14

Original release date:

2017-09-11

Authors:

Crusca, E.; Munte, C.

Citation:

Citation: Vicente, E.; Sahu, I.; Costa-Filho, A.; Cilli, E.; Lorigan, G.. "Conformational changes of the HsDHODH N-terminal Microdomain via DEER Spectroscopy." J. Phys. Chem. B 119, 8693-8697 (2015).
PubMed: 26086954

Assembly members:

Assembly members:
Dihydroorotate dehydrogenase (quinone), mitochondrial, polymer, 35 residues, 3831.320 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: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Dihydroorotate dehydrogenase (quinone), mitochondrial: GDERFYAEHLMPTLQGLLDP ESAHRLAVRFTSLGX

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	51
15N chemical shifts	32
1H chemical shifts	235

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 35 residues - 3831.320 Da.

1

GLY

ASP

GLU

ARG

PHE

TYR

ALA

GLU

HIS

LEU

2

MET

PRO

THR

LEU

GLN

GLY

LEU

ASP

PRO

3

GLU

SER

ALA

HIS

ARG

LEU

ALA

VAL

ARG

PHE

4

THR

SER

LEU

GLY

NH2

Samples:

sample_1: peptide 700 uM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0 mM; pH: 7.4; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D DQF-COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

NMRView, Johnson, One Moon Scientific - chemical shift assignment, chemical shift calculation, data analysis, peak picking

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

Bruker AvanceIII 600 MHz
Bruker AvanceIII 800 MHz

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