BMRB Entry 30661

Title:
Solution NMR Structure Of The Full Length Latent Form MinE Protein From Neisseria gonorrheae
Deposition date:
2019-08-30
Original release date:
2020-07-05
Authors:
Cai, M.; Shen, Y.; Clore, M.
Citation:

Citation: Cai, Mengli; Huang, Ying; Shen, Yang; Li, Min; Mizuuchi, Michiyo; Ghirlando, Rodolfo; Mizuuchi, Kiyoshi; Clore, G Marius. "Probing transient excited states of the bacterial cell division regulator MinE by relaxation dispersion NMR spectroscopy"  Proc Natl Acad Sci U S A 116, 25446-25455 (2019).
PubMed: 31772021

Assembly members:

Assembly members:
entity_1, polymer, 81 residues, 9256.723 Da.

Natural source:

Natural source:   Common Name: Neisseria gonorrhoeae   Taxonomy ID: 485   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Neisseria gonorrhoeae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: PET-30A

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts236
15N chemical shifts77
1H chemical shifts147

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1, 11
2entity_1, 21

Entities:

Entity 1, entity_1, 1 81 residues - 9256.723 Da.

1   METSERLEUILEGLULEULEUPHEGLYGLN
2   METGLNLYSTHRALATHRVALALAARGASP
3   ARGLEUGLNILEILEILEALAGLNGLUARG
4   ALAGLNGLUGLYGLNTHRPROASPTYRLEU
5   PROTHRLEUARGLYSALALEUMETGLUVAL
6   LEUSERLYSTYRVALASNVALSERLEUASP
7   ASNILEARGILESERGLNGLULYSGLNASP
8   GLYMETASPVALLEUGLULEUASNILETHR
9   LEU

Samples:

sample_1: MinE-wt, [U-13C; U-15N], 1.0 mM; potassium phosphate 25 mM; EDTA 0.5 mM; benzamidine chloride 0.1 mM

sample_2: MinE-wt-RDC, [U-2H; U-15N], 1.0 mM

sample_3: MinE-d10, [U-13C; U-15N], 1.0 mM; potassium phosphate 25 mM; EDTA 0.5 mM; benzamidine chloride 0.1 mM

sample_4: MinE-d10-RDC, [U-2H; U-15N], 1.0 mM; MinE-d10-CPMG, [U-2H; U-15N], 1.0 mM

sample_conditions_1: ionic strength: 25 mM; pH: 6.5; pressure: 1 bar; temperature: 298 K

sample_conditions_2: ionic strength: 200 mM; pH: 6.5; pressure: 1 bar; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CBCACO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HBHA(CBCACO)NHsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
HSQC IPAPsample_2anisotropicsample_conditions_2
HSQC IPAPsample_2isotropicsample_conditions_2
HSQC IPAPsample_4anisotropicsample_conditions_2
HSQC IPAPsample_4isotropicsample_conditions_2

Software:

PIPP, Garrett - chemical shift assignment, peak picking

CS-ROSETTA, Shen, Vernon, Baker and Bax - refinement, structure calculation

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

NMR spectrometers:

  • Bruker AVANCE 500 MHz
  • Bruker AVANCE 600 MHz
  • Bruker AVANCE 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks