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 15776

Title: Pfu Rpp21 structure and assignments   PubMed: 18922021

Deposition date: 2008-05-15 Original release date: 2008-11-14

Authors: Amero, Carlos; Foster, Mark; Boomershine, William; Xu, Yiren

Citation: Amero, Carlos; Boomershine, William; Xu, Yiren; Foster, Mark. "Solution structure of Pyrococcus furiosus RPP21, a component of the archaeal RNase P holoenzyme, and interactions with its RPP29 protein partner"  Biochemistry 47, 11704-11710 (2008).

Assembly members:
Rpp21, polymer, 123 residues, 65.409 Da.
ZN, non-polymer, 65.409 Da.

Natural source:   Common Name: Pyrococcus furiosus   Taxonomy ID: 2261   Superkingdom: Archaea   Kingdom: not available   Genus/species: Pyrococcus furiosus

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

Entity Sequences (FASTA):
Rpp21: MAKYNEKKEKKRIAKERIDI LFSLAERVFPYSPELAKRYV ELALLVQQKAKVKIPRKWKR RYCKKCHAFLVPGINARVRL RQKRMPHIVVKCLECGHIMR YPYIKEIKKRRKEKMEYGGL VPR

Data sets:
Data typeCount
13C chemical shifts370
15N chemical shifts75
1H chemical shifts558

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Related Database Links:

PDB 2K3R 2KI7
GB AAL81737 AFN05027
REF WP_011012760
SP Q8U0H6

Download simulated HSQC data in one of the following formats:
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