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 27564

Title: 1H, 13C, 15N NMR Backbone assignments of B. cereus 5/B/6 metallo-beta-lactamase   PubMed: 31009467

Deposition date: 2018-07-30 Original release date: 2018-09-04

Authors: Khan, Nazmul; Shaw, Robert; Latham, Michael

Citation: Khan, Nazmul; Bui, Anthony; Xiao, Yang; Sutton, Roger; Wylie, Benjamin; Latham, Michael; Shaw, Robert. "A DNA aptamer reveals an allosteric site for inhibition in metallo-beta-lactamases"  PLoS One 14, .-e0214440 (e0214440).

Assembly members:
metallo-beta-lactamase, polymer, 227 residues, Formula weight is not available
ZINC ION, non-polymer, 65.409 Da.

Natural source:   Common Name: Bacillus cereus   Taxonomy ID: 1396   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus cereus

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

Entity Sequences (FASTA):
metallo-beta-lactamase: ERTVEHKVIKNETGTISISQ LNKNVWVHTELGYFSGEAVP SNGLVLNTSKGLVLVDSSWD DKLTKELIEMVEKKFKKRVT DVIITHAHADRIGGMKTLKE RGIKAHSTALTAELAKKNGY EEPLGDLQSVTNLKFGNMKV ETFYPGKGHTEDNIVVWLPQ YQILAGGCLVKSASSKDLGN VADAYVNEWSTSIENVLKRY GNINLVVPGHGEVGDRGLLL HTLDLLK

Data sets:
Data typeCount
13C chemical shifts566
15N chemical shifts199
1H chemical shifts199

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1metallo-beta-lactamase1
2Zn2+ ions, 12
3Zn2+ ions, 22

Entities:

Entity 1, metallo-beta-lactamase 227 residues - Formula weight is not available

1   GLUARGTHRVALGLUHISLYSVALILELYS
2   ASNGLUTHRGLYTHRILESERILESERGLN
3   LEUASNLYSASNVALTRPVALHISTHRGLU
4   LEUGLYTYRPHESERGLYGLUALAVALPRO
5   SERASNGLYLEUVALLEUASNTHRSERLYS
6   GLYLEUVALLEUVALASPSERSERTRPASP
7   ASPLYSLEUTHRLYSGLULEUILEGLUMET
8   VALGLULYSLYSPHELYSLYSARGVALTHR
9   ASPVALILEILETHRHISALAHISALAASP
10   ARGILEGLYGLYMETLYSTHRLEULYSGLU
11   ARGGLYILELYSALAHISSERTHRALALEU
12   THRALAGLULEUALALYSLYSASNGLYTYR
13   GLUGLUPROLEUGLYASPLEUGLNSERVAL
14   THRASNLEULYSPHEGLYASNMETLYSVAL
15   GLUTHRPHETYRPROGLYLYSGLYHISTHR
16   GLUASPASNILEVALVALTRPLEUPROGLN
17   TYRGLNILELEUALAGLYGLYCYSLEUVAL
18   LYSSERALASERSERLYSASPLEUGLYASN
19   VALALAASPALATYRVALASNGLUTRPSER
20   THRSERILEGLUASNVALLEULYSARGTYR
21   GLYASNILEASNLEUVALVALPROGLYHIS
22   GLYGLUVALGLYASPARGGLYLEULEULEU
23   HISTHRLEUASPLEULEULYS

Entity 2, Zn2+ ions, 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: 5/B/6 MBL, [U-100% 13C; U-100% 15N], 1.4 mM

sample_conditions_1: ionic strength: 0.001 M; pH: 7; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

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

VNMRJ, Varian - collection

Analysis, CCPN - chemical shift assignment

NMR spectrometers:

  • Agilent DD2 600 MHz

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