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 34122

Title: Solution NMR Structure of the C-terminal domain of ParB (Spo0J)   PubMed: 29244022

Deposition date: 2017-04-11 Original release date: 2017-12-11

Authors: Higman, V.; Fisher, G.; Dillingham, M.; Crump, M.

Citation: Fisher, G.; Pastrana, C.; Higman, V.; Koh, A.; Taylor, J.; Butterer, A.; Craggs, T.; Sobott, F.; Murray, H.; Crump, M.; Moreno-Herrero, F.; Dillingham, M.. "The structural basis for dynamic DNA binding and bridging interactions which condense the bacterial centromere."  Elife 6, e28086-e28086 (2017).

Assembly members:
entity_1, polymer, 69 residues, 8111.201 Da.

Natural source:   Common Name: Bacillus subtilis   Taxonomy ID: 1423   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus subtilis

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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts642
15N chemical shifts150
1H chemical shifts1030

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Entity Assembly IDEntity NameEntity ID
1entity_1, 11
2entity_1, 21


Entity 1, entity_1, 1 69 residues - 8111.201 Da.



sample_3: ParB (Spo0J) 1.5 mM; sodium chloride 137 mM; potassium chloride 2.7 mM; Na2HPO4 10 mM; KH2PO4 1.8 mM; ParB (Spo0J)-label, [U-13C; U-15N], 1.5 mM

sample_1: ParB (Spo0J) 3 mM; sodium chloride 137 mM; potassium chloride 2.7 mM; Na2HPO4 10 mM; KH2PO4 1.8 mM

sample_2: ParB (Spo0J), [U-13C; U-15N], 3 mM; sodium chloride 137 mM; potassium chloride 2.7 mM; Na2HPO4 10 mM; KH2PO4 1.8 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.1; pressure: 1 atm; temperature: 208 K


NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2not availablesample_conditions_1
2D 1H-13C HSQCsample_2not availablesample_conditions_1
3D HNCOsample_2not availablesample_conditions_1
3D HNCAsample_2not availablesample_conditions_1
3D HN(CO)CAsample_2not availablesample_conditions_1
3D HNCACBsample_2not availablesample_conditions_1
3D CBCA(CO)NHsample_2not availablesample_conditions_1
3D C(CO)NHsample_2not availablesample_conditions_1
3D H(CCO)NHsample_2not availablesample_conditions_1
3D HCCH-TOCSYsample_2not availablesample_conditions_1
3D 1H-15N NOESYsample_2not availablesample_conditions_1
3D 1H-13C NOESY aliphaticsample_2not availablesample_conditions_1
3D 1H-13C NOESY aromaticsample_2not availablesample_conditions_1
2D 1H-1H TOCSYsample_1not availablesample_conditions_1
2D 1H-1H NOESYsample_1not availablesample_conditions_1
3D 13C,15N F1-filtered, 13C,15N F3-edited 13C-NOSEY-HSQCsample_3not availablesample_conditions_1
3D 13C,15N F1-filtered, 13C,15N F3-edited 15N-NOSEY-HSQCsample_3not availablesample_conditions_1


NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

Analysis, CCPN - chemical shift assignment, peak picking

TALOS, Cornilescu, Delaglio and Bax - data analysis

ARIA, Linge, O'Donoghue and Nilges - structure calculation

NMR spectrometers:

  • Varian VNMRS 600 MHz

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