BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 17775

Title: Solution structure of the chimeric Af1503 HAMP- EnvZ DHp homodimer   PubMed: 22244755

Deposition date: 2011-07-10 Original release date: 2011-08-16

Authors: Coles, Murray; Ferris, Hedda; Hulko, Michael; Martin, Joerg; Lupas, Andrei

Citation: Ferris, Hedda; Dunin-Horkawicz, Stanislaw; Hornig, Nora; Hulko, Michael; Martin, Jorg; Schultz, Joachim; Zeth, Kornelius; Lupas, Andrei; Coles, Murray. "Mechanism of regulation of receptor histidine kinases."  Structure 20, 56-66 (2012).

Assembly members:
HAMP-DHp, polymer, 112 residues, 12738.506 Da.

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

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

Entity Sequences (FASTA):
HAMP-DHp: MSTITRPIIELSNTADKIAE GNLEAEVPHQNRADEIGILA KSIERLRRSLKQLADDRTLL MAGVSHDLRTPLTRIRLATE MMSEQDGYLAESINKDIEEC NAIIEQFIDYLR

Data sets:
Data typeCount
13C chemical shifts456
15N chemical shifts112
1H chemical shifts758

Additional metadata:

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

Related Database Links:

UNP P0AEJ4 O28769
BMRB 17776
PDB 2LFR 2LFS 3ZCC 3ZRV 3ZRW 3ZRX 4CTI
GB ESL47213

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