BMRB Entry 25924

Name: Drosha Quad
Published: 2016-12-15

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PDB ID: 2na2
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25924
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:

Drosha Quad

Deposition date:

2015-12-17

Original release date:

2016-12-15

Authors:

Showalter, Scott; Sahu, Debashish; Kranick, Joshua

Citation:

Citation: Kranick, Joshua; Chadalavada, Durga; Sahu, Debashish; Showalter, Scott. "Engineering double-stranded RNA binding activity into the Drosha double-stranded RNA binding domain results in a loss of microRNA processing function" PLoS ONE 12, e0182445-e0182445 (2017).
PubMed: 28792523

Assembly members:

Assembly members:
entity, polymer, 82 residues, 8973.405 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: pET49b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GPGNDPISQLQQCCLTLRTE GKEPDIPLYKTLQTVGPSHA RTYTVAVYFKGERIGCGKGP SKKQAKMGAAMDALEKYNFP QM

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	298
15N chemical shifts	67
1H chemical shifts	356

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 82 residues - 8973.405 Da.

1

GLY

PRO

GLY

ASN

ASP

PRO

ILE

SER

GLN

LEU

2

GLN

CYS

LEU

THR

LEU

ARG

THR

GLU

3

GLY

LYS

GLU

PRO

ASP

ILE

PRO

LEU

TYR

LYS

4

THR

LEU

GLN

THR

VAL

GLY

PRO

SER

HIS

ALA

5

ARG

THR

TYR

THR

VAL

ALA

VAL

TYR

PHE

LYS

6

GLY

GLU

ARG

ILE

GLY

CYS

GLY

LYS

GLY

PRO

7

SER

LYS

GLN

ALA

LYS

MET

GLY

ALA

8

MET

ASP

ALA

LEU

GLU

LYS

TYR

ASN

PHE

PRO

9

GLN

MET

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 850 mM; cacodylate pH 7.29 100 mM; potassium chloride 100 mM; beta-mercaptoethanol 5 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 0.1 M; pH: 7.29; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D (H)CCO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.5, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - chemical shift calculation

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 500 MHz

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