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 15642

Title: Solution structure of the aminoterminal domain of E. coli NusG   PubMed: 19500594

Deposition date: 2008-01-25 Original release date: 2009-06-10

Authors: Schweimer, Kristian; Scheckenhofer, Ulrich; Roesch, Paul

Citation: Mooney, Rachel Anne; Schweimer, Kristian; Roesch, Paul; Gottesman, Max; Landick, Robert. "Two structurally independent domains of E. coli NusG create regulatory plasticity via distinct interactions with RNA polymerase and regulators."  J. Mol. Biol. 391, 341-358 (2009).

Assembly members:
NusG, polymer, 123 residues, 14096.366 Da.

Natural source:   Common Name: not available   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):
NusG: MSEAPKKRWYVVQAFSGFEG RVATSLREHIKLHNMEDLFG EVMVPTEEVVEIRGGQRRKS ERKFFPGYVLVQMVMNDASW HLVRSVPRVMGFIGGTSDRP APISDKEVDAIMNRLQQVGD KPR

Data sets:
Data typeCount
13C chemical shifts498
15N chemical shifts122
1H chemical shifts790

Additional metadata:

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

BMRB 15490
PDB 2JVV 2K06
DBJ BAB38328 BAE73404 BAE77338 BAG79793 BAH61119
EMBL CAD09492 CAG73137 CAH19518 CAL10413 CAL22339
GB AAA24622 AAC43080 AAC76956 AAF33495 AAG59178
PIR AB0934
REF NP_312932 NP_418409 NP_457922 NP_463017 NP_709777
SP P0AA01 P0AA02 P0AA03 P0AFG0 P0AFG1

Download simulated HSQC data in one of the following formats:
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