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 6745

Title: Backbone 1H, 13C, and 15N chemical shift assignments of human HnRNP F   PubMed: 16341757

Deposition date: 2005-07-25 Original release date: 2005-12-20

Authors: Dominguez, Cyril; Allain, Frederic

Citation: Dominguez, Cyril; Allain, Frederic. "Resonance Assignments of the Two N-terminal RNA Recognition Motifs (RRM) of the Human Heterogeneous Nuclear Ribonucleoprotein F (HnRNP F)"  J. Biomol. NMR 33, 282-282 (2005).

Assembly members:
Heterogeneous nuclear ribonucleoprotein F, RRM domains 1 and 2, polymer, 194 residues, 21655 Da.

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

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
Heterogeneous nuclear ribonucleoprotein F, RRM domains 1 and 2: MMLGPEGGEGFVVKLRGLPW SCSVEDVQNFLSDCTIHDGA AGVHFIYTREGRQSGEAFVE LGSEDDVKMALKKDRESMGH RYIEVFKSHRTEMDWVLKHS GPNSADSANDGFVRLRGLPF GCTKEEIVQFFSGLEIVPNG ITLPVDPEGKITGEAFVQFA SQELAEKALGKHKERIGHRY IEVFKSSQEEVRSY

Data sets:
Data typeCount
13C chemical shifts443
15N chemical shifts190
1H chemical shifts1237

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HnRNP F RRM121

Entities:

Entity 1, HnRNP F RRM12 194 residues - 21655 Da.

1   METMETLEUGLYPROGLUGLYGLYGLUGLY
2   PHEVALVALLYSLEUARGGLYLEUPROTRP
3   SERCYSSERVALGLUASPVALGLNASNPHE
4   LEUSERASPCYSTHRILEHISASPGLYALA
5   ALAGLYVALHISPHEILETYRTHRARGGLU
6   GLYARGGLNSERGLYGLUALAPHEVALGLU
7   LEUGLYSERGLUASPASPVALLYSMETALA
8   LEULYSLYSASPARGGLUSERMETGLYHIS
9   ARGTYRILEGLUVALPHELYSSERHISARG
10   THRGLUMETASPTRPVALLEULYSHISSER
11   GLYPROASNSERALAASPSERALAASNASP
12   GLYPHEVALARGLEUARGGLYLEUPROPHE
13   GLYCYSTHRLYSGLUGLUILEVALGLNPHE
14   PHESERGLYLEUGLUILEVALPROASNGLY
15   ILETHRLEUPROVALASPPROGLUGLYLYS
16   ILETHRGLYGLUALAPHEVALGLNPHEALA
17   SERGLNGLULEUALAGLULYSALALEUGLY
18   LYSHISLYSGLUARGILEGLYHISARGTYR
19   ILEGLUVALPHELYSSERSERGLNGLUGLU
20   VALARGSERTYR

Samples:

sample_1: HnRNP F RM12, [U-13C; U-15N], 0.4 mM; NaH2PO4 25 mM; NaCl 50 mM

conditions_1: ionic strength: 0.075 M; pH: 6.2; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D (15N-1H)-HSQCsample_1not availableconditions_1
2D (13C-1H)-HSQCsample_1not availableconditions_1
3D HNCAsample_1not availableconditions_1
3D HNCACBsample_1not availableconditions_1
3D HN(CO)CAsample_1not availableconditions_1
3D CBCA(CO)NHsample_1not availableconditions_1
3D H(C)CH-TOCSYsample_1not availableconditions_1
3D (H)CCH-TOCSYsample_1not availableconditions_1
3D NOESY-(15N-1H)-HSQCsample_1not availableconditions_1
3D NOESY-(13C-1H)-HSQCsample_1not availableconditions_1
2D (1H-1H)-TOCSYsample_1not availableconditions_1
2D (1H-1H)-NOESYsample_1not availableconditions_1

Software:

No software information available

NMR spectrometers:

  • Bruker AVANCE 900 MHz
  • Bruker DRX 500 MHz
  • Bruker DRX 600 MHz

Related Database Links:

REF XP_004607668

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