BMRB Entry 50546

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50546

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Backbone 1H,13C, and 15N Chemical Shift Assignments for the Toho-1 b-lactamase R274N/R276N double mutant enzyme
Deposition date:
2020-11-04
Original release date:
2021-07-27
Authors:
Mueller, Leonard; Sakhrani, Varun; Coates, Leighton; Weiss, Kevin
Citation:

Citation: Sakhrani, Varun; Ghosh, Rittik; Hilario, Eduardo; Weiss, Kevin; Coates, Leighton; Mueller, Leonard. "Toho-1 beta-lactamase: backbone chemical shift assignments and changes in dynamics upon binding with avibactam"  J. Biomol. NMR 75, 303-318 (2021).
PubMed: 34218390

Assembly members:

Assembly members:
entity_1, polymer, 263 residues, 28660 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pJexpress401

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MANSVQQQLEALEKSSGGRL GVALINTADNSQILYRADER FAMCSTSKVMAAAAVLKQSE SDKHLLNQRVEIKKSDLVNY NPIAEKHVNGTMTLAELGAA ALQYSDNTAMNKLIAHLGGP DKVTAFARSLGDETFRLDRT EPTLNTAIPGDPRDTTTPLA MAQTLKNLTLGKALAETQRA QLVTWLKGNTTGSASIRAGL PKSWVVGDKTGSGDYGTTND IAVIWPENHAPLVLVTYFTQ PEQKAENRNDILAAAAKIVT HGF

Data sets:
Data typeCount
13C chemical shifts739
15N chemical shifts241
1H chemical shifts241

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1A Toho-1 b-lactamase R274N/R276N double mutant1

Entities:

Entity 1, A Toho-1 b-lactamase R274N/R276N double mutant 263 residues - 28660 Da.

The sequence for Toho-1 b-lactamase starts at residue 25 and ends, after 263 residues and three gaps (positions 58, 239, and 253), at residue 290.

1   METALAASNSERVALGLNGLNGLNLEUGLU
2   ALALEUGLULYSSERSERGLYGLYARGLEU
3   GLYVALALALEUILEASNTHRALAASPASN
4   SERGLNILELEUTYRARGALAASPGLUARG
5   PHEALAMETCYSSERTHRSERLYSVALMET
6   ALAALAALAALAVALLEULYSGLNSERGLU
7   SERASPLYSHISLEULEUASNGLNARGVAL
8   GLUILELYSLYSSERASPLEUVALASNTYR
9   ASNPROILEALAGLULYSHISVALASNGLY
10   THRMETTHRLEUALAGLULEUGLYALAALA
11   ALALEUGLNTYRSERASPASNTHRALAMET
12   ASNLYSLEUILEALAHISLEUGLYGLYPRO
13   ASPLYSVALTHRALAPHEALAARGSERLEU
14   GLYASPGLUTHRPHEARGLEUASPARGTHR
15   GLUPROTHRLEUASNTHRALAILEPROGLY
16   ASPPROARGASPTHRTHRTHRPROLEUALA
17   METALAGLNTHRLEULYSASNLEUTHRLEU
18   GLYLYSALALEUALAGLUTHRGLNARGALA
19   GLNLEUVALTHRTRPLEULYSGLYASNTHR
20   THRGLYSERALASERILEARGALAGLYLEU
21   PROLYSSERTRPVALVALGLYASPLYSTHR
22   GLYSERGLYASPTYRGLYTHRTHRASNASP
23   ILEALAVALILETRPPROGLUASNHISALA
24   PROLEUVALLEUVALTHRTYRPHETHRGLN
25   PROGLUGLNLYSALAGLUASNARGASNASP
26   ILELEUALAALAALAALALYSILEVALTHR
27   HISGLYPHE

Samples:

sample_1: Toho-1 b-lactamase R274N/R276N double mutant enzyme, [U-13C; U-15N; U-2H], 825 uM; sodium azide 0.05%; EDTA 1 mM; DTT 1 mM; MES Buffer 20 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

SPARKY - chemical shift assignment

CcpNMR - chemical shift assignment

PINE - chemical shift assignment

TOPSPIN v3.6 - processing

NMR spectrometers:

  • Bruker AVANCE III 700 MHz

Related Database Links:

PDB

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks