BMRB Entry 34259

Name: Solution structure of FUS-RRM bound to stem-loop RNA
Published: 2019-03-15

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PDB ID: 6gbm
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34259
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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 FUS-RRM bound to stem-loop RNA

Deposition date:

2018-04-15

Original release date:

2019-03-15

Authors:

Loughlin, F.; Allain, F.

Citation:

Citation: Loughlin, F.; Lukavsky, P.; Kazeeva, T.; Reber, S.; Hock, E.; Colombo, M.; Von Schroetter, C.; Pauli, P.; Clery, A.; Muhlemann, O.; Polymenidou, M.; Ruepp, M.; Allain, F.. "The Solution Structure of FUS Bound to RNA Reveals a Bipartite Mode of RNA Recognition with Both Sequence and Shape Specificity." Mol. Cell 73, 490-504 (2019).
PubMed: 30581145

Assembly members:

Assembly members:
entity_1, polymer, 102 residues, 11289.521 Da.
entity_2, polymer, 23 residues, 7286.336 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMDNSDNNTIFVQGLGEN VTIESVADYFKQIGIIKTNK KTGQPMINLYTDRETGKLKG EATVSFDDPPSAKAAIDWFD GKEFSGNPIKVSFATRRADF NR
entity_2: GGCAGAUUACAAUUCUAUUU GCC

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
- assigned_chemical_shifts_2
spectral_peak_list

Data type	Count
13C chemical shifts	479
15N chemical shifts	120
1H chemical shifts	901

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	2

Entities:

Entity 1, entity_1 102 residues - 11289.521 Da.

1

GLY

SER

HIS

MET

ASP

ASN

SER

ASP

ASN

2

THR

ILE

PHE

VAL

GLN

GLY

LEU

GLY

GLU

ASN

3

VAL

THR

ILE

GLU

SER

VAL

ALA

ASP

TYR

PHE

4

LYS

GLN

ILE

GLY

ILE

LYS

THR

ASN

LYS

5

LYS

THR

GLY

GLN

PRO

MET

ILE

ASN

LEU

TYR

6

THR

ASP

ARG

GLU

THR

GLY

LYS

LEU

LYS

GLY

7

GLU

ALA

THR

VAL

SER

PHE

ASP

PRO

8

SER

ALA

LYS

ALA

ILE

ASP

TRP

PHE

ASP

9

GLY

LYS

GLU

PHE

SER

GLY

ASN

PRO

ILE

LYS

10

VAL

SER

PHE

ALA

THR

ARG

ALA

ASP

PHE

11

ASN

ARG

Entity 2, entity_2 23 residues - 7286.336 Da.

1

G

C

A

G

A

U

A

C

2

A

U

C

U

A

U

3

G

C

Samples:

sample_1: FUS-RRM, [U-99% 13C; U-99% 15N], 0.8 mM; RNA stem loop, [U-99% 15N], 0.8 mM; sodium phosphate 20 mM; beta-mercaptoethanol 1 mM

sample_2: FUS-RRM, [U-99% 13C; U-99% 15N], 0.8 mM; sodium phosphate 20 mM; beta-mercaptoethanol 1 mM; stem-loop RNA, [U-99% 15N], 0.8 mM

sample_3: FUS-RRM, [U-99% 15N], 1 mM; sodium phosphate 20 mM; beta-mercaptoethanol 1 mM; stem-loop RNA, [U-99% 13C; U-99% 15N], 0.8 mM

sample_4: FUS-RRM, [U-99% 15N], 1.0 mM; sodium phosphate 20 mM; beta-mercaptoethanol 1 mM; stem-loop RNA, [U-99% 13C; U-99% 15N], 0.8 mM

sample_5: FUS-RRM, [U-99% 15N], 1.0 mM; sodium phosphate 20 mM; beta-mercaptoethanol 1 mM; stem-loop RNA, [U-99% 15N], 1.0 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6.5; pressure: 1 Pa; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_4	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_4	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_5	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_4	isotropic	sample_conditions_1

Software:

AMBER, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

SPARKY, Goddard - data analysis

CANDID, Herrmann, Guntert and Wuthrich - peak picking

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

Bruker Avance 900 MHz
Bruker AvanceIII 700 MHz

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