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 17989

Title: NMR resonance assignment of the UUP protein C-terminal domain   PubMed: 22287065

Deposition date: 2011-10-11 Original release date: 2012-01-31

Authors: Carlier, Ludovic; Haase, Sander; Lequin, Olivier

Citation: Carlier, Ludovic; Haase, A. Sander; Burgos Zepeda, Monica; Dassa, Elie; Lequin, Olivier. "Secondary structure and NMR resonance assignments of the C-terminal DNA-binding domain of Uup protein."  Biomol. NMR Assignments 6, 197-200 (2012).

Assembly members:
UUP, polymer, 112 residues, 12563 Da.

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

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

Entity Sequences (FASTA):
UUP: GSHMGQQEQYVALKQPAVKK TEEAAAAKAETVKRSSSKLS YKLQRELEQLPQLLEDLEAK LEALQTQVADASFFSQPHEQ TQKVLADMAAAEQELEQAFE RWEYLEALKNGG

Data sets:
Data typeCount
13C chemical shifts478
15N chemical shifts113
1H chemical shifts771

Additional metadata:

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

PDB 2LW1
DBJ BAA35707 BAB34456 BAG76534 BAI24392 BAI29842
EMBL CAA70589 CAP75412 CAQ31477 CAQ88615 CAQ97854
GB AAC74035 AAG55435 AAN42579 AAN79553 AAP16463
REF NP_309060 NP_415469 NP_706872 WP_000053029 WP_000053031
SP P43672

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