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 30322

Title: NMR solution structure of a-lytic protease 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:
Alpha-lytic protease, polymer, 198 residues, 19875.131 Da.

Natural source:   Common Name: Lysobacter enzymogenes   Taxonomy ID: 69   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Lysobacter enzymogenes

Experimental source:   Production method: .

Entity Sequences (FASTA):
Alpha-lytic protease: ANIVGGIEYSINNASLCSVG FSVTRGATKGFVTAGHCGTV NATARIGGAVVGTFAARVFP GNDRAWVSLTSAQTLLPRVA NGSSFVTVRGSTEAAVGAAV CRSGRTTGYQCGTITAKNVT ANYAEGAVRGLTQGNACMGR GDSGGSWITSAGQAQGVMSG GNVQSNGNNCGIPASQRSSL FERLQPILSQYGLSLVTG

Data sets:
Data typeCount
13C chemical shifts540
15N chemical shifts222
1H chemical shifts1201

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 198 residues - 19875.131 Da.

1   ALAASNILEVALGLYGLYILEGLUTYRSER
2   ILEASNASNALASERLEUCYSSERVALGLY
3   PHESERVALTHRARGGLYALATHRLYSGLY
4   PHEVALTHRALAGLYHISCYSGLYTHRVAL
5   ASNALATHRALAARGILEGLYGLYALAVAL
6   VALGLYTHRPHEALAALAARGVALPHEPRO
7   GLYASNASPARGALATRPVALSERLEUTHR
8   SERALAGLNTHRLEULEUPROARGVALALA
9   ASNGLYSERSERPHEVALTHRVALARGGLY
10   SERTHRGLUALAALAVALGLYALAALAVAL
11   CYSARGSERGLYARGTHRTHRGLYTYRGLN
12   CYSGLYTHRILETHRALALYSASNVALTHR
13   ALAASNTYRALAGLUGLYALAVALARGGLY
14   LEUTHRGLNGLYASNALACYSMETGLYARG
15   GLYASPSERGLYGLYSERTRPILETHRSER
16   ALAGLYGLNALAGLNGLYVALMETSERGLY
17   GLYASNVALGLNSERASNGLYASNASNCYS
18   GLYILEPROALASERGLNARGSERSERLEU
19   PHEGLUARGLEUGLNPROILELEUSERGLN
20   TYRGLYLEUSERLEUVALTHRGLY

Samples:

sample_1: alpha-lytic protease protein, [U-13C; U-15N], 2.0 mM; sodium acetate 10 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 4.0; 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:

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

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

SPARKY, Goddard - peak picking

NMR spectrometers:

  • Bruker AvanceIII 950 MHz

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