BMRB Entry 19976

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19976

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Title:
1H, 13C and 15N backbone resonance assignments for beta-lactamase BlaP with proline-glycine inserted at position 197
Deposition date:
2014-05-16
Original release date:
2019-07-11
Authors:
Thorn, David; Dumoulin, Mireille; Damblon, Christian
Citation:

Citation: Thorn, David; Kay, Jennifer; Rhazi, Noureddine; Dumoulin, Mireille; Corazza, Alessandra; Damblon, Christian. "1H, 13C and 15N backbone resonance assignments of the beta-lactamase BlaP from Bacillus licheniformis 749/C and two mutational variants"  Biomol. NMR Assign. 12, 69-77 (2018).
PubMed: 29030803

Assembly members:

Assembly members:
BlaP197, polymer, 273 residues, 30368.2276 Da.

Natural source:

Natural source:   Common Name: firmicutes   Taxonomy ID: 1402   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus licheniformis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BlaP197: TEMKDDFAKLEEQFDAKLGI FALDTGTNRTVAYRPDERFA FASTIKALTVGVLLQQKSIE DLNQRITYTRDDLVNYNPIT EKHVDTGMTLKELADASLRY SDNAAQNLILKQIGGPESLK KELRKIGDEVTNPERFEPEL NEVNPGETQDTSTARALVTS LRAFALEDPGKLPSEKRELL IDWMKRNTTGDALIRAGVPD GWEVADKTGAASYGTRNDIA IIWPPKGDPVVLAVLSSRDK KDAKYDDKLIAEATKVVMKA LNMNGKGPHHHHH

Data sets:
Data typeCount
13C chemical shifts746
15N chemical shifts244
1H chemical shifts244

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BlaP1971

Entities:

Entity 1, BlaP197 273 residues - 30368.2276 Da.

1   THRGLUMETLYSASPASPPHEALALYSLEU
2   GLUGLUGLNPHEASPALALYSLEUGLYILE
3   PHEALALEUASPTHRGLYTHRASNARGTHR
4   VALALATYRARGPROASPGLUARGPHEALA
5   PHEALASERTHRILELYSALALEUTHRVAL
6   GLYVALLEULEUGLNGLNLYSSERILEGLU
7   ASPLEUASNGLNARGILETHRTYRTHRARG
8   ASPASPLEUVALASNTYRASNPROILETHR
9   GLULYSHISVALASPTHRGLYMETTHRLEU
10   LYSGLULEUALAASPALASERLEUARGTYR
11   SERASPASNALAALAGLNASNLEUILELEU
12   LYSGLNILEGLYGLYPROGLUSERLEULYS
13   LYSGLULEUARGLYSILEGLYASPGLUVAL
14   THRASNPROGLUARGPHEGLUPROGLULEU
15   ASNGLUVALASNPROGLYGLUTHRGLNASP
16   THRSERTHRALAARGALALEUVALTHRSER
17   LEUARGALAPHEALALEUGLUASPPROGLY
18   LYSLEUPROSERGLULYSARGGLULEULEU
19   ILEASPTRPMETLYSARGASNTHRTHRGLY
20   ASPALALEUILEARGALAGLYVALPROASP
21   GLYTRPGLUVALALAASPLYSTHRGLYALA
22   ALASERTYRGLYTHRARGASNASPILEALA
23   ILEILETRPPROPROLYSGLYASPPROVAL
24   VALLEUALAVALLEUSERSERARGASPLYS
25   LYSASPALALYSTYRASPASPLYSLEUILE
26   ALAGLUALATHRLYSVALVALMETLYSALA
27   LEUASNMETASNGLYLYSGLYPROHISHIS
28   HISHISHIS

Samples:

sample_1: BlaP197, [U-100% 13C; U-100% 15N], 0.8 mM; H2O 95%; D2O 5%; sodium phosphate 20 mM; NaCl 50 mM

Standard: ionic strength: 0.070 M; pH: 6.5; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicStandard
3D HN(CO)CAsample_1isotropicStandard
2D 1H-15N HSQC/HMQCsample_1isotropicStandard
3D HNCACBsample_1isotropicStandard
HNcoCACB (H[N[co[{CA|ca[C]}]]])sample_1isotropicStandard
HNCO (H[N[trho(N)][CO]])sample_1isotropicStandard
HNcaCO (H[N[ca[CO]]])sample_1isotropicStandard

Software:

CcpNmr_Analysis v2.3.1, CCPN - assignment, data analysis

TOPSPIN v2.1, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 500 MHz

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