BMRB Entry 16194

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

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PDB ID: 2kg1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16194
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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 third 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.
third qRRM of hnRNP F, polymer, 105 residues, 11508.767 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
third qRRM of hnRNP F: GDSEFTVQSTTGHCVHMRGL PYKATENDIYNFFSPLNPVR VHIEIGPDGRVTGEADVEFA THEEAVAAMSKDRANMQHRY IELFLNSTTGASNGAYSSQV MQGMG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	283
15N chemical shifts	114
1H chemical shifts	700

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	third qRRM of hnRNP F	2

Entities:

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

1

A

G

A

U

Entity 2, third qRRM of hnRNP F 105 residues - 11508.767 Da.

1

GLY

ASP

SER

GLU

PHE

THR

VAL

GLN

SER

THR

2

THR

GLY

HIS

CYS

VAL

HIS

MET

ARG

GLY

LEU

3

PRO

TYR

LYS

ALA

THR

GLU

ASN

ASP

ILE

TYR

4

ASN

PHE

SER

PRO

LEU

ASN

PRO

VAL

ARG

5

VAL

HIS

ILE

GLU

ILE

GLY

PRO

ASP

GLY

ARG

6

VAL

THR

GLY

GLU

ALA

ASP

VAL

GLU

PHE

ALA

7

THR

HIS

GLU

ALA

VAL

ALA

MET

SER

8

LYS

ASP

ARG

ALA

ASN

MET

GLN

HIS

ARG

TYR

9

ILE

GLU

LEU

PHE

LEU

ASN

SER

THR

GLY

10

ALA

SER

ASN

GLY

ALA

TYR

SER

GLN

VAL

11

MET

GLN

GLY

MET

GLY

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: 293 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, 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

PDB	2HGN 2KG1
DBJ	BAM09220
GB	AAH23162 AEB61257 EGW08331