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 5315

Title: 1H, 13C and 15N chemical shift assignment for ribosome-associated factor Y   PubMed: 12392550

Deposition date: 2002-03-08 Original release date: 2003-02-20

Authors: Ye, Keqiong; Serganov, Alexander; Hu, Weidong; Patel, Dinshaw

Citation: Ye, Keqiong; Serganov, Alexander; Hu, Weidong; Patel, Dinshaw. "Ribosome-associated Factor Y adopts a Fold resembling a Double-stranded RNA Binding Domain Scaffold "  Eur. J. Biochem. 269, 5182-5191 (2002).

Assembly members:
Protein Yfia, polymer, 112 residues, Formula weight is not available

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
Protein Yfia: TMNITSKQMEITPAIRQHVA DRLAKLEKWQTHLINPHIIL SKEPQGFVADATINTPNGVL VASGKHEDMYTAINELINKL ERQLNKLQHKGEARRAATSV KDANFVEEVEEE

Data sets:
Data typeCount
1H chemical shifts818
13C chemical shifts499
15N chemical shifts120
coupling constants75

Additional metadata:

  • Assembly
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  • Spectrometers
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Related Database Links:

BMRB 5389
PDB 1L4S 1N3G 1VOQ 1VOS 1VOV 1VOX 1VOZ 3V2C 3V2E
DBJ BAA16481 BAB36883 BAG78406 BAI26837 BAI31922
EMBL CAA94436 CAP77041 CAQ32967 CAQ88030 CAQ99546
GB AAA24328 AAC75646 AAG57709 AAN44153 AAN81568
REF NP_289151 NP_311487 NP_417088 NP_708446 NP_755000
SP P0AD49 P0AD50 P0AD51 P0AD52

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