BMRB Entry 34344

Title:
NMR structure of BB_P28, Borrelia burgdorferi outer surface lipoprotein
Deposition date:
2018-12-21
Original release date:
2020-01-24
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:
Surface protein, mlp lipoprotein family, polymer, 102 residues, 11038.109 Da.

Natural source:

Natural source:   Common Name: Borreliella burgdorferi   Taxonomy ID: 224326   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Borreliella Borreliella burgdorferi

Experimental source:

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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts414
15N chemical shifts114
1H chemical shifts677

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 102 residues - 11038.109 Da.

1   GLYALAMETGLYPROLYSSERLYSGLUGLU
2   LEULEUARGGLULYSLEUSERGLUASPGLN
3   LYSTHRHISLEUASPTRPLEULYSGLUALA
4   LEUGLYASNASPGLYGLUPHEASPLYSPHE
5   LEUGLYTYRASPGLUSERLYSILELYSTHR
6   ALALEUASPHISILELYSSERGLULEUASP
7   LYSCYSASNGLYASNASPALAASPGLNGLN
8   LYSTHRTHRPHELYSGLNTHRVALGLNGLY
9   ALALEUSERGLYGLYILEASPGLYPHEGLY
10   SERASNASNALAVALTHRTHRCYSGLYASN
11   GLYSER

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:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CANDID v2.02, Herrmann, Guntert and Wuthrich - structure calculation

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, peak picking

TOPSPIN v3.5, Bruker Biospin - 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