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 25003

Title: 1H, 13C and 15N backbone resonance assignments for the class A beta-lactamase BlaP from Bacillus licheniformis 749/C with proline-glycine inserted at position 216   PubMed: 29030803

Deposition date: 2014-06-06 Original release date: 2019-07-11

Authors: Kay, Jennifer; Thorn, David; Dumoulin, Mireille; Damblon, Christian; Corazza, Alessandra

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).

Assembly members:
BlaP216Q0, polymer, 273 residues, 30368.3 Da.

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

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

Entity Sequences (FASTA):
BlaP216Q0: TEMKDDFAKLEEQFDAKLGI FALDTGTNRTVAYRPDERFA FASTIKALTVGVLLQQKSIE DLNQRITYTRDDLVNYNPIT EKHVDTGMTLKELADASLRY SDNAAQNLILKQIGGPESLK KELRKIGDEVTNPERFEPEL NEVNPGETQDTSTARALVTS LRAFALEDKLPSEKRELLID WMKRNTTPGGDALIRAGVPD GWEVADKTGAASYGTRNDIA IIWPPKGDPVVLAVLSSRDK KDAKYDDKLIAEATKVVMKA LNMNGKGPHHHHH

Data sets:
Data typeCount
13C chemical shifts765
15N chemical shifts255
1H chemical shifts253

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1BlaP216Q01

Entities:

Entity 1, BlaP216Q0 273 residues - 30368.3 Da.

Residues 267-273 (FASTA sequence) represent a non-native tag

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   LEUARGALAPHEALALEUGLUASPLYSLEU
18   PROSERGLULYSARGGLULEULEUILEASP
19   TRPMETLYSARGASNTHRTHRPROGLYGLY
20   ASPALALEUILEARGALAGLYVALPROASP
21   GLYTRPGLUVALALAASPLYSTHRGLYALA
22   ALASERTYRGLYTHRARGASNASPILEALA
23   ILEILETRPPROPROLYSGLYASPPROVAL
24   VALLEUALAVALLEUSERSERARGASPLYS
25   LYSASPALALYSTYRASPASPLYSLEUILE
26   ALAGLUALATHRLYSVALVALMETLYSALA
27   LEUASNMETASNGLYLYSGLYPROHISHIS
28   HISHISHIS

Samples:

sample_1: BlaP216Q0, [U-100% 13C; U-100% 15N], 0.6 mM; Sodium Phosphate 20 mM; NaCl 50 mM; H2O 95%; D2O 5%

Standard: ionic strength: 0.063 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[trho(N)][CO]])sample_1isotropicStandard
HNcaCO(H[N[ca[CO]]])sample_1isotropicStandard

Software:

SPARKY v3.113, Goddard - chemical shift assignment

TOPSPIN v2.1, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 500 MHz

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