BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16193

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

Authors: Allain, Frederic; Dominguez, Cyril

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:
AGGGAU G-tract RNA, polymer, 6 residues, 1955.251 Da.
second qRRM of hnRNP F, polymer, 92 residues, 10228.562 Da.

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):
AGGGAU G-tract RNA: AGGGAU
second qRRM of hnRNP F: NSADSANDGFVRLRGLPFGC TKEEIVQFFSGLEIVPNGIT LPVDPEGKITGEAFVQFASQ ELAEKALGKHKERIGHRYIE VFKSSQEEVRSY

Data sets:
Data typeCount
13C chemical shifts357
15N chemical shifts97
1H chemical shifts680

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

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

Entities:

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

1   AGGGAU

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

1   ASNSERALAASPSERALAASNASPGLYPHE
2   VALARGLEUARGGLYLEUPROPHEGLYCYS
3   THRLYSGLUGLUILEVALGLNPHEPHESER
4   GLYLEUGLUILEVALPROASNGLYILETHR
5   LEUPROVALASPPROGLUGLYLYSILETHR
6   GLYGLUALAPHEVALGLNPHEALASERGLN
7   GLULEUALAGLULYSALALEUGLYLYSHIS
8   LYSGLUARGILEGLYHISARGTYRILEGLU
9   VALPHELYSSERSERGLNGLUGLUVALARG
10   SERTYR

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:

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 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

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