BMRB Entry 50328

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50328

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Title:
BBP28 reduced 23-148
Deposition date:
2020-06-16
Original release date:
2020-11-03
Authors:
Fridmanis, J.; Otikovs, M.; Brangulis, K.; Jaudzems, K.
Citation:

Citation: Fridmanis, Jekabs; Otikovs, Martins; Brangulis, Kalvis; Tars, Kaspars; Jaudzems, Kristaps. "Solution NMR structure of Borrelia burgdorferi outer surface lipoprotein BBP28, a member of the mlp protein family"  Proteins: Struct. Funct. Bioinf. 89, 588-594 (2021).
PubMed: 32949018

Assembly members:

Assembly members:
entity_1, polymer, 130 residues, 14205.61 Da.

Natural source:

Natural source:   Common Name: Borrelia burgdorferi   Taxonomy ID: 139   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Borrelia burgdorferi

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: pETM11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMGNDTLKNNAQQTKSRGK RDLTQKEATPEKPKSKEELL REKLSEDQKTHLDWLKEALG NDGEFDKFLGYDESKIKTAL DHIKSELDKCNGNDADQQKT TFKQTVQGALSGGIDGFGSN NAVTTCGNGS

Data sets:
Data typeCount
13C chemical shifts322
15N chemical shifts106
1H chemical shifts106

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 130 residues - 14205.61 Da.

1   GLYALAMETGLYASNASPTHRLEULYSASN
2   ASNALAGLNGLNTHRLYSSERARGGLYLYS
3   ARGASPLEUTHRGLNLYSGLUALATHRPRO
4   GLULYSPROLYSSERLYSGLUGLULEULEU
5   ARGGLULYSLEUSERGLUASPGLNLYSTHR
6   HISLEUASPTRPLEULYSGLUALALEUGLY
7   ASNASPGLYGLUPHEASPLYSPHELEUGLY
8   TYRASPGLUSERLYSILELYSTHRALALEU
9   ASPHISILELYSSERGLULEUASPLYSCYS
10   ASNGLYASNASPALAASPGLNGLNLYSTHR
11   THRPHELYSGLNTHRVALGLNGLYALALEU
12   SERGLYGLYILEASPGLYPHEGLYSERASN
13   ASNALAVALTHRTHRCYSGLYASNGLYSER

Samples:

sample_1: sodium phosphate 20 ± 1 mM; sodium chloride 50 ± 1 mM; sodium azide 0.03 ± 0.0001 % w/v; EDTA 1 ± 0.01 mM; BB_P28, [U-13C; U-15N], 2 ± 0.1 mM

sample_conditions_1: ionic strength: 0.08 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

CARA v1.8.4 - chemical shift assignment, peak picking

TOPSPIN v3.5 - collection

NMR spectrometers:

  • Varian Unity 600 MHz

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