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 30325

Title: NMR solution structure of KanY protein (ms6282) using two 4D-spectra   PubMed: 29374165

Deposition date: 2017-08-03 Original release date: 2018-01-29

Authors: Evangelidis, T.; Nerli, S.; Sgourakis, N.; Tripsianes, K.

Citation: Evangelidis, T.; Nerli, S.; Novacek, J.; Brereton, A.; Karplus, P.; Dotas, R.; Venditti, V.; Sgourakis, N.; Tripsianes, K.. "Automated NMR resonance assignments and structure determination using a minimal set of 4D spectra"  Nat. Commun. 9, 384-384 (2018).

Assembly members:
Uncharacterized protein, polymer, 145 residues, 15285.261 Da.

Natural source:   Common Name: Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)   Taxonomy ID: 246196   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycobacterium smegmatis

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

Entity Sequences (FASTA):
Uncharacterized protein: MGQVSAVSTVLINAEPAAVL AAISDYQTVRPKILSSHYSG YQVLEGGQGAGTVATWKLQA TKSRVRDVKATVDVAGHTVI EKDANSSLVSNWTVAPAGTG SSVNLKTTWTGAGGVKGFFE KTFAPLGLRRIQDEVLENLK KHVEG

Data sets:
Data typeCount
13C chemical shifts445
15N chemical shifts152
1H chemical shifts959

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 145 residues - 15285.261 Da.

1   METGLYGLNVALSERALAVALSERTHRVAL
2   LEUILEASNALAGLUPROALAALAVALLEU
3   ALAALAILESERASPTYRGLNTHRVALARG
4   PROLYSILELEUSERSERHISTYRSERGLY
5   TYRGLNVALLEUGLUGLYGLYGLNGLYALA
6   GLYTHRVALALATHRTRPLYSLEUGLNALA
7   THRLYSSERARGVALARGASPVALLYSALA
8   THRVALASPVALALAGLYHISTHRVALILE
9   GLULYSASPALAASNSERSERLEUVALSER
10   ASNTRPTHRVALALAPROALAGLYTHRGLY
11   SERSERVALASNLEULYSTHRTHRTRPTHR
12   GLYALAGLYGLYVALLYSGLYPHEPHEGLU
13   LYSTHRPHEALAPROLEUGLYLEUARGARG
14   ILEGLNASPGLUVALLEUGLUASNLEULYS
15   LYSHISVALGLUGLY

Samples:

sample_1: KanY protein ms6282, [U-13C; U-15N], 1.2 mM; sodium phosphate 50 mM; NaCl 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
4D HC(CC TOCSY(CO))NHsample_1isotropicsample_conditions_1
4D 13C,15N edited HMQC-NOESY-HSQCsample_1isotropicsample_conditions_1
4D 13C,13C edited HMQC-NOESY-HSQCsample_1isotropicsample_conditions_1

Software:

CS-Rosetta, Shen, Vernon, Baker and Bax - data analysis, refinement, structure calculation

SPARKY, Goddard - peak picking

4D-CHAINS, Evangelidis and Tripsianes - chemical shift assignment

NMR spectrometers:

  • Bruker AvanceIII 850 MHz

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