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 25821

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

Deposition date: 2015-09-18 Original release date: 2019-07-10

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

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:
BlaPdPG, polymer, 271 residues, 30214.1 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-28b

Entity Sequences (FASTA):
BlaPdPG: TEMKDDFAKLEEQFDAKLGI FALDTGTNRTVAYRPDERFA FASTIKALTVGVLLQQKSIE DLNQRITYTRDDLVNYNPIT EKHVDTGMTLKELADASLRY SDNAAQNLILKQIGGPESLK KELRKIGDEVTNPERFEPEL NEVNPGETQDTSTARALVTS LRAFALEDKLPSEKRELLID WMKRNTTGDALIRAGVPDGW EVADKTGAASYGTRNDIAII WPPKGDPVVLAVLSSRDKKD AKYDDKLIAEATKVVMKALN MNGKGPHHHHH

Data sets:
Data typeCount
13C chemical shifts251
15N chemical shifts251
1H chemical shifts251

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1BlaPdPG1

Entities:

Entity 1, BlaPdPG 271 residues - 30214.1 Da.

Residues 265-271 (FASTA sequence) represent a non-native tag -GP(His)5 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   TRPMETLYSARGASNTHRTHRGLYASPALA
20   LEUILEARGALAGLYVALPROASPGLYTRP
21   GLUVALALAASPLYSTHRGLYALAALASER
22   TYRGLYTHRARGASNASPILEALAILEILE
23   TRPPROPROLYSGLYASPPROVALVALLEU
24   ALAVALLEUSERSERARGASPLYSLYSASP
25   ALALYSTYRASPASPLYSLEUILEALAGLU
26   ALATHRLYSVALVALMETLYSALALEUASN
27   METASNGLYLYSGLYPROHISHISHISHIS
28   HIS

Samples:

sample_1: BlaPdPG, [U-100% 13C; U-100% 15N], 0.48 mM; sodium phosphate 20 mM; sodium chloride 50 mM

Standard: ionic strength: 0.063 M; pH: 6.5; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicStandard
3D HNCAsample_1isotropicStandard
3D HN(CO)CAsample_1isotropicStandard

Software:

CCPN vv.2.4.1, CCPN - chemical shift assignment, data analysis

TOPSPIN v2.1, Bruker Biospin - collection, processing

NMR spectrometers:

  • 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