BMRB Entry 30322

Title:
NMR solution structure of a-lytic protease using two 4D-spectra
Deposition date:
2017-08-03
Original release date:
2018-01-29
Authors:
Evangelidis, T.; Nerli, S.; Sgourakis, N.; Tripsianes, K.
Citation:

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).
PubMed: 29374165

Assembly members:

Assembly members:
Alpha-lytic protease, polymer, 198 residues, 19875.131 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: .

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

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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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

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