BMRB Entry 16194

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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
MolProbity Validation Chart

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

Additional metadata:

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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

Related Database Links:

PDB 2HGN 2KG1
DBJ BAM09220
GB AAH23162 AEB61257 EGW08331

Download HSQC peak lists in one of the following formats:
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