BMRB Entry 16193

Name: Structure of the second qRRM domain of hnRNP F in complex with a AGGGAU G-tract RNA
Published: 2010-06-15

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PDB ID: 2kg0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16193
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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:

Structure of the second qRRM domain of hnRNP F in complex with a AGGGAU G-tract RNA

Deposition date:

2009-03-02

Original release date:

2010-06-15

Authors:

Allain, Frederic; Dominguez, Cyril

Citation:

Citation: Dominguez, Cyril; Fisette, Jean-Francois; Chabot, Benoit; Allain, Frederic. "Structural basis of G-tract recognition and encaging by hnRNP F quasi-RRMs." Nat. Struct. Mol. Biol. 17, 853-861 (2010).
PubMed: 20526337

Assembly members:

Assembly members:
AGGGAU G-tract RNA, polymer, 6 residues, 1955.251 Da.
second qRRM of hnRNP F, polymer, 92 residues, 10228.562 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):
AGGGAU G-tract RNA: AGGGAU
second qRRM of hnRNP F: NSADSANDGFVRLRGLPFGC TKEEIVQFFSGLEIVPNGIT LPVDPEGKITGEAFVQFASQ ELAEKALGKHKERIGHRYIE VFKSSQEEVRSY

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	357
15N chemical shifts	97
1H chemical shifts	680

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	AGGGAU G-tract RNA	1
2	second qRRM of hnRNP F	2

Entities:

Entity 1, AGGGAU G-tract RNA 6 residues - 1955.251 Da.

1

A

G

A

U

Entity 2, second qRRM of hnRNP F 92 residues - 10228.562 Da.

1

ASN

SER

ALA

ASP

SER

ALA

ASN

ASP

GLY

PHE

2

VAL

ARG

LEU

ARG

GLY

LEU

PRO

PHE

GLY

CYS

3

THR

LYS

GLU

ILE

VAL

GLN

PHE

SER

4

GLY

LEU

GLU

ILE

VAL

PRO

ASN

GLY

ILE

THR

5

LEU

PRO

VAL

ASP

PRO

GLU

GLY

LYS

ILE

THR

6

GLY

GLU

ALA

PHE

VAL

GLN

PHE

ALA

SER

GLN

7

GLU

LEU

ALA

GLU

LYS

ALA

LEU

GLY

LYS

HIS

8

LYS

GLU

ARG

ILE

GLY

HIS

ARG

TYR

ILE

GLU

9

VAL

PHE

LYS

SER

GLN

GLU

VAL

ARG

10

SER

TYR

Samples:

sample_1: entity_11 – 1.5 mM; entity_2, [U-13C; U-15N], 1 – 1.5 mM; NaH2PO4 20 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 70 mM; pH: 7.0; pressure: 1 atm; temperature: 303 K

Experiments:

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 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

SPARKY v3.113, Goddard - chemical shift assignment

CYANA v2.1, Herrmann, Guntert and Wuthrich - structure solution

AMBER v7.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

NMR spectrometers:

Bruker Avance 500 MHz
Bruker Avance 600 MHz
Bruker Avance 700 MHz
Bruker Avance 900 MHz