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Biological Magnetic Resonance Data Bank


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BMRB Entry 34379

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34379

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Title: Solution structure of sortase A from S. aureus in complex with 2-(aminomethyl)-3-hydroxy-4H-pyran-4-one based prodrug

Deposition date: 2019-03-15 Original release date: 2020-01-17

Authors: Jaudzems, K.; Leonchiks, A.

Citation: Jaudzems, K.. "Solution structure of sortase A from S. aureus in complex with 2-(aminomethyl)-3-hydroxy-4H-pyran-4-one based prodrug"  . ., .-..

Assembly members:
entity_1, polymer, 148 residues, 16825.062 Da.
entity_JPT, non-polymer, 240.276 Da.

Natural source:   Common Name: Staphylococcus aureus subsp. aureus NCTC 8325   Taxonomy ID: 93061   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Staphylococcus aureus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
entity_1: MQAKPQIPKDKSKVAGYIEI PDADIKEPVYPGPATPEQLN RGVSFAEENESLDDQNISIA GHTFIDRPNYQFTNLKAAKK GSMVYFKVGNETRKYKMTSI RDVKPTDVEVLDEQKGKDKQ LTLITCDDYNEKTGVWEKRK IFVATEVK

Data sets:
Data typeCount
13C chemical shifts663
15N chemical shifts149
1H chemical shifts1055

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 148 residues - 16825.062 Da.

1   METGLNALALYSPROGLNILEPROLYSASP
2   LYSSERLYSVALALAGLYTYRILEGLUILE
3   PROASPALAASPILELYSGLUPROVALTYR
4   PROGLYPROALATHRPROGLUGLNLEUASN
5   ARGGLYVALSERPHEALAGLUGLUASNGLU
6   SERLEUASPASPGLNASNILESERILEALA
7   GLYHISTHRPHEILEASPARGPROASNTYR
8   GLNPHETHRASNLEULYSALAALALYSLYS
9   GLYSERMETVALTYRPHELYSVALGLYASN
10   GLUTHRARGLYSTYRLYSMETTHRSERILE
11   ARGASPVALLYSPROTHRASPVALGLUVAL
12   LEUASPGLUGLNLYSGLYLYSASPLYSGLN
13   LEUTHRLEUILETHRCYSASPASPTYRASN
14   GLULYSTHRGLYVALTRPGLULYSARGLYS
15   ILEPHEVALALATHRGLUVALLYS

Entity 2, entity_2 - C11 H10 O4 S - 240.276 Da.

1   JPT

Samples:

sample_1: Sortase A protein, [U-13C; U-15N], 1.6 ± 0.2 mM; 3-hydroxy-6-(hydroxymethyl)-2-(thiophen-3-ylmethyl)-4H-pyran-4-one 3.2 ± 0.2 mM; sodium acetate 20 ± 2 mM; sodium chloride 50 ± 5 mM; calcium chloride 10 ± 1 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D (F1)-15N,13C-filtered 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D (F1,F2)-13C,15N-filtered NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D (F1,F2)-13C,15N-filtered TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

CYANA, Guntert, Mumenthaler and Wuthrich - data analysis

TOPSPIN, Bruker Biospin - processing

VNMR v2.1b, Varian - collection

CARA v1.9, Keller and Wuthrich - chemical shift assignment

UNIO, T. Herrmann, F. Fiorito, J. Volk - data analysis, peak picking

NMR spectrometers:

  • Varian INOVA 600 MHz

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