BMRB Entry 19928

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19928

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Title:
Chemical shift assignments BamA-P4P5
Deposition date:
2014-04-22
Original release date:
2016-01-11
Authors:
Houben, Klaartje; Sinnige, Tessa; Pritisanac, Iva; Daniels, Mark; Boelens, Rolf; Baldus, Marc
Citation:

Citation: Sinnige, Tessa; Weingarth, Markus; Daniels, Mark; Boelens, Rolf; Bonvin, Alexandre; Houben, Klaartje; Baldus, Marc. "Conformational Plasticity of the POTRA 5 Domain in the Outer Membrane Protein Assembly Factor BamA"  Structure 23, 1317-1324 (2015).
PubMed: 26027731

Assembly members:

Assembly members:
BamA-P4P5, polymer, 167 residues, 18800 Da.

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: pLICHIS

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BamA-P4P5: GSLTEGDQYKLSGVEVSGNL AGHSAEIEQLTKIEPGELYN GTKVTKMEDDIKKLLGRYGY AYPRVQSMPEINDADKTVKL RVNVDAGNRFYVRKIRFEGN DTSKDAVLRREMRQMEGAWL GSDLVDQGKERLNRLGFFET VDTDTQRVPGSPDQVDVVYK VKERNTG

Data sets:
Data typeCount
13C chemical shifts654
15N chemical shifts175
1H chemical shifts983

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1P4P51

Entities:

Entity 1, P4P5 167 residues - 18800 Da.

residues 258-260 (GSL) are residues left after cleaving of the HIS6-tag with thrombin

1   GLYSERLEUTHRGLUGLYASPGLNTYRLYS
2   LEUSERGLYVALGLUVALSERGLYASNLEU
3   ALAGLYHISSERALAGLUILEGLUGLNLEU
4   THRLYSILEGLUPROGLYGLULEUTYRASN
5   GLYTHRLYSVALTHRLYSMETGLUASPASP
6   ILELYSLYSLEULEUGLYARGTYRGLYTYR
7   ALATYRPROARGVALGLNSERMETPROGLU
8   ILEASNASPALAASPLYSTHRVALLYSLEU
9   ARGVALASNVALASPALAGLYASNARGPHE
10   TYRVALARGLYSILEARGPHEGLUGLYASN
11   ASPTHRSERLYSASPALAVALLEUARGARG
12   GLUMETARGGLNMETGLUGLYALATRPLEU
13   GLYSERASPLEUVALASPGLNGLYLYSGLU
14   ARGLEUASNARGLEUGLYPHEPHEGLUTHR
15   VALASPTHRASPTHRGLNARGVALPROGLY
16   SERPROASPGLNVALASPVALVALTYRLYS
17   VALLYSGLUARGASNTHRGLY

Samples:

sample_1: BamA-P4P5, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 50 mM; sodium chloride 100 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 150 mM; pH: 6.25; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D HccneHEsample_1isotropicsample_conditions_1
2D hCcneHEsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 600 MHz

Related Database Links:

UniprotKB A7ZWC3

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