BMRB Entry 25831

Name: solution structure of the complex of microRNA 20b pre-element with Rbfox RRM
Published: 2016-04-12

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PDB ID: 2n82
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25831
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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:

solution structure of the complex of microRNA 20b pre-element with Rbfox RRM

Deposition date:

2015-09-30

Original release date:

2016-04-12

Authors:

Yang, Fan; Chen, Yu; Varani, Gabriele

Citation:

Citation: Chen, Yu; Zubovic, Lorena; Yang, Fan; Godin, Katherine; Pavelitz, Tom; Castellanos, Javier; Macchi, Paolo; Varani, Gabriele. "Rbfox proteins regulate microRNA biogenesis by sequence-specific binding to their precursors and target downstream Dicer" Nucleic Acids Res. 44, 4381-4395 (2016).
PubMed: 27001519

Assembly members:

Assembly members:
miR-20b, polymer, 23 residues, 7318.388 Da.
Rbfox_RRM, polymer, 104 residues, Formula weight is not available

Natural source:

Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: T7 in vitro transcription Host organism: NA Vector: NA

Entity Sequences (FASTA):

Entity Sequences (FASTA):
miR-20b: GGUAGUUUUGGCAUGACUCU ACC
Rbfox_RRM: GSHMNTENKSQPKRLHVSNI PFRFRDPDLRQMFGQFGKIL DVEIIFNERGSKGFGFVTFE NSADADRAREKLHGTVVEGR KIEVNNATARVMTNKKTVNP YTNG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2

Data type	Count
13C chemical shifts	566
15N chemical shifts	115
1H chemical shifts	838

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	miR-20b	1
2	Rbfox_RRM	2

Entities:

Entity 1, miR-20b 23 residues - 7318.388 Da.

1

G

U

A

G

U

G

2

G

C

A

U

G

A

C

U

C

U

3

A

C

Entity 2, Rbfox_RRM 104 residues - Formula weight is not available

1

GLY

SER

HIS

MET

ASN

THR

GLU

ASN

LYS

SER

2

GLN

PRO

LYS

ARG

LEU

HIS

VAL

SER

ASN

ILE

3

PRO

PHE

ARG

PHE

ARG

ASP

PRO

ASP

LEU

ARG

4

GLN

MET

PHE

GLY

GLN

PHE

GLY

LYS

ILE

LEU

5

ASP

VAL

GLU

ILE

PHE

ASN

GLU

ARG

GLY

6

SER

LYS

GLY

PHE

GLY

PHE

VAL

THR

PHE

GLU

7

ASN

SER

ALA

ASP

ALA

ASP

ARG

ALA

ARG

GLU

8

LYS

LEU

HIS

GLY

THR

VAL

GLU

GLY

ARG

9

LYS

ILE

GLU

VAL

ASN

ALA

THR

ALA

ARG

10

VAL

MET

THR

ASN

LYS

THR

VAL

ASN

PRO

11

TYR

THR

ASN

GLY

Name	Sample	Sample state	Sample conditions
2D F1-, F2-filtered 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D F1-, F2-filtered 1H-1H NOESY	sample_2	isotropic	sample_conditions_2
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_2
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_2
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_2
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_2
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_2
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_2
3D HNCACB	sample_1	isotropic	sample_conditions_2
3D HNCO	sample_1	isotropic	sample_conditions_2
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_2
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_2
3D CCH-TOCSY	sample_2	isotropic	sample_conditions_2
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_2
3D 1H-13C NOESY	sample_3	isotropic	sample_conditions_2
2D 1H-15N HSQC	sample_4	isotropic	sample_conditions_1
3D 13C F1-filtered, F3-edited NOESY-HSQC	sample_2	isotropic	sample_conditions_2

BMRB Entry 25831

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: