BMRB Entry 15917

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15917

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Title:
TEM-1 BETA-LACTAMASE VARIANT ALLOSTERICALLY REGULATED BY KANAMYCIN
Deposition date:
2008-08-13
Original release date:
2012-03-13
Authors:
Volkov, Alexander; Ubbink, Marcellus; Soumillion, Patrice
Citation:

Citation: Volkov, Alexander; Barrios, Humberto; Mathonet, Pascale; Evrard, Christine; Ubbink, Marcellus; Declercq, Jean-Paul; Soumillion, Patrice; Fastrez, Jacques. "Engineering an allosteric binding site for aminoglycosides into TEM1-beta-Lactamase"  Chembiochem 12, 904-913 (2011).
PubMed: 21425229

Assembly members:

Assembly members:
blaKR, polymer, 269 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET24

Entity Sequences (FASTA):

Entity Sequences (FASTA):
blaKR: HPETLVKVKDAEDQLCRTSH RPCRVGYIELDLNSGKILES FRPEERFPMMSTFKVLLCGA VLSRIDAGQEQLGRRIHYSQ NDLVKYSPVTEKHLTDGMTV RELCSAAITMSDNTAANLLL TTIGGPKELTAFLHNMGDHV TRLDRWEPELNEAIPNDERD TTMPVAMATTLRKLLTGELL TLASRQQLIDWMEADKVAGP LLRSALPAGWFIADKSGAGR RGSRGIIAALGPDGKPSRIV VIYTTGSRKKTDERNRQIAE IGASLIKHW

Data sets:
Data typeCount
13C chemical shifts735
15N chemical shifts487
1H chemical shifts487

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1beta-lactamase1

Entities:

Entity 1, beta-lactamase 269 residues - Formula weight is not available

1   HISPROGLUTHRLEUVALLYSVALLYSASP
2   ALAGLUASPGLNLEUCYSARGTHRSERHIS
3   ARGPROCYSARGVALGLYTYRILEGLULEU
4   ASPLEUASNSERGLYLYSILELEUGLUSER
5   PHEARGPROGLUGLUARGPHEPROMETMET
6   SERTHRPHELYSVALLEULEUCYSGLYALA
7   VALLEUSERARGILEASPALAGLYGLNGLU
8   GLNLEUGLYARGARGILEHISTYRSERGLN
9   ASNASPLEUVALLYSTYRSERPROVALTHR
10   GLULYSHISLEUTHRASPGLYMETTHRVAL
11   ARGGLULEUCYSSERALAALAILETHRMET
12   SERASPASNTHRALAALAASNLEULEULEU
13   THRTHRILEGLYGLYPROLYSGLULEUTHR
14   ALAPHELEUHISASNMETGLYASPHISVAL
15   THRARGLEUASPARGTRPGLUPROGLULEU
16   ASNGLUALAILEPROASNASPGLUARGASP
17   THRTHRMETPROVALALAMETALATHRTHR
18   LEUARGLYSLEULEUTHRGLYGLULEULEU
19   THRLEUALASERARGGLNGLNLEUILEASP
20   TRPMETGLUALAASPLYSVALALAGLYPRO
21   LEULEUARGSERALALEUPROALAGLYTRP
22   PHEILEALAASPLYSSERGLYALAGLYARG
23   ARGGLYSERARGGLYILEILEALAALALEU
24   GLYPROASPGLYLYSPROSERARGILEVAL
25   VALILETYRTHRTHRGLYSERARGLYSLYS
26   THRASPGLUARGASNARGGLNILEALAGLU
27   ILEGLYALASERLEUILELYSHISTRP

Samples:

sample_1: blaKR, [U-99% 13C; U-99% 15N], 0.6 mM; sodium phosphate 20 mM; H2O 93%; D2O, [U-100% 2H], 7%

sample_2: blaKR, [U-99% 15N], 0.6 mM; MES 20 mM; H2O 93%; D2O, [U-100% 2H], 7%

sample_conditions_1: ionic strength: 35 mM; pH: 6.6; pressure: 1 atm; temperature: 303 K

sample_conditions_2: ionic strength: 20 mM; pH: 6.6; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_2

Software:

TOPSPIN, Bruker Biospin - collection

AZARA, Boucher - peak picking, processing

ANSIG, Kraulis - chemical shift assignment

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

PDB
DBJ GAN11567
GB AAA64566 AAB60535 ABG56555 ABG56563 ABG56577
REF WP_003520151

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