BMRB Entry 18393

Name: The second dsRBD domain from A. thaliana DICER-LIKE 1
Published: 2013-01-22

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PDB ID: 2lrs
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18393
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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:

The second dsRBD domain from A. thaliana DICER-LIKE 1

Deposition date:

2012-04-12

Original release date:

2013-01-22

Authors:

Burdisso, Paula; Suarez, Irina; Bersch, Beate; Bologna, Nicolas; Palatnik, Javier; Boisbouvier, Jerome; Rasia, Rodolfo

Citation:

Citation: Burdisso, Paula; Suarez, Irina; Bologna, Nicolas; Palatnik, Javier; Bersch, Beate; Rasia, Rodolfo. "Second double-stranded RNA binding domain of dicer-like ribonuclease 1: structural and biochemical characterization." Biochemistry 51, 10159-10166 (2012).
PubMed: 23194006

Assembly members:

Assembly members:
dsRBD, polymer, 71 residues, 7961.290 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 Vector: pET-TEV

Entity Sequences (FASTA):

Entity Sequences (FASTA):
dsRBD: NDICLRKNWPMPSYRCVKEG GPAHAKRFTFGVRVNTSDRG WTDECIGEPMPSVKKAKDSA AVLLLELLNKT

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	309
15N chemical shifts	67
1H chemical shifts	475

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	dsRBD	1

Entities:

Entity 1, dsRBD 71 residues - 7961.290 Da.

1

ASN

ASP

ILE

CYS

LEU

ARG

LYS

ASN

TRP

PRO

2

MET

PRO

SER

TYR

ARG

CYS

VAL

LYS

GLU

GLY

3

GLY

PRO

ALA

HIS

ALA

LYS

ARG

PHE

THR

PHE

4

GLY

VAL

ARG

VAL

ASN

THR

SER

ASP

ARG

GLY

5

TRP

THR

ASP

GLU

CYS

ILE

GLY

GLU

PRO

MET

6

PRO

SER

VAL

LYS

ALA

LYS

ASP

SER

ALA

7

ALA

VAL

LEU

GLU

LEU

ASN

LYS

8

THR

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_4	isotropic	sample_conditions_2and3
3D HNCA	sample_4	isotropic	sample_conditions_2and3
3D HNCACB	sample_4	isotropic	sample_conditions_2and3
3D HN(CO)CA	sample_4	isotropic	sample_conditions_2and3
3D HN(CO)CACB	sample_4	isotropic	sample_conditions_2and3
3D HN(CA)CO	sample_4	isotropic	sample_conditions_2and3
3D HN(CA)HA	sample_4	isotropic	sample_conditions_2and3
3D H(CCO)NH	sample_4	isotropic	sample_conditions_2and3
3D HCCH-TOCSY	sample_4	isotropic	sample_conditions_2and3
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_3	isotropic	sample_conditions_2and3
2D 1H-1H TOCSY	sample_3	isotropic	sample_conditions_2and3
2D 15N-IPAP-HSQC	sample_2	anisotropic	sample_conditions_2and3
3D HNHA	sample_4	isotropic	sample_conditions_2and3

PDB	2LRS
DBJ	BAD94606
EMBL	CDX90002 CDY15207
GB	AAF03534 AAF26461 AAG38019 AAG38020 AEE27220
REF	NP_001184881 NP_171612 XP_002892088 XP_006306578 XP_006418369
SP	Q9SP32
AlphaFold	Q9SP32

BMRB Entry 18393

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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