BMRB Entry 16194

Title:
Structure of the third qRRM domain of hnRNP F in complex with a AGGGAU G-tract RNA   PubMed: 20526337
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).

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:   Production method: chemical synthesis

Experimental source:

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

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts283
15N chemical shifts114
1H chemical shifts700

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1AGGGAU G-tract RNA1
2third qRRM of hnRNP F2

Entities:

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

1   AGGGAU

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

1   GLYASPSERGLUPHETHRVALGLNSERTHR
2   THRGLYHISCYSVALHISMETARGGLYLEU
3   PROTYRLYSALATHRGLUASNASPILETYR
4   ASNPHEPHESERPROLEUASNPROVALARG
5   VALHISILEGLUILEGLYPROASPGLYARG
6   VALTHRGLYGLUALAASPVALGLUPHEALA
7   THRHISGLUGLUALAVALALAALAMETSER
8   LYSASPARGALAASNMETGLNHISARGTYR
9   ILEGLULEUPHELEUASNSERTHRTHRGLY
10   ALASERASNGLYALATYRSERSERGLNVAL
11   METGLNGLYMETGLY

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_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

Related Database Links:

PDB
DBJ BAM09220
GB AAH23162 AEB61257 EGW08331

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts