BMRB Entry 31293

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31293
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
Solution structure of the surface domain of the Borrelia burgdorferi outer surface lipoprotein BBA36
Deposition date:
2026-02-06
Original release date:
2026-10-29
Authors:
Buchko, G.; Keough, M.; Ewasechko, N.; Patel, D.; Olmedo, D.; Chaconas, G.; Savchenko, A.; Seattle Structural Genomics Center for Infectious Disease (SSGCID), SSGCID
Citation:

Citation: Buchko, G.; Keough, M.; Ewasechko, N.; Patel, D.; Olmedo, D.; Chaconas, G.; Savchenko, A.; Seattle Structural Genomics Center for Infectious Disease (SSGCID), SSGCID. "Solution structure of the surface domain of the Borrelia burgdorferi outer surface lipoprotein BBA36 "  .

Assembly members:

Assembly members:
entity_1, polymer, 187 residues, 21573.213 Da.

Natural source:

Natural source:   Common Name: Lyme disease spirochete   Taxonomy ID: 139   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Borreliella burgdorferi

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MHHHHHHSSGVDLGTENLYF QSNEISLTPEEAEKLESLKV FLKDAMSVNGREEALKAEYE KSYKEFFDWLSKDVNRQKEF ISSFDNISSIVSKAVDASKK RRPTEQQSLGFKEYVCYKIK NSKGEALSLFFQKVVDAFGA DPYKKDNDESVQKPVKCNEE IFKVIKKVLTESESNNELKN LKNYGNV

Data sets:
Data typeCount
13C chemical shifts609
15N chemical shifts170
1H chemical shifts905

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 187 residues - 21573.213 Da.

1   METHISHISHISHISHISHISSERSERGLY
2   VALASPLEUGLYTHRGLUASNLEUTYRPHE
3   GLNSERASNGLUILESERLEUTHRPROGLU
4   GLUALAGLULYSLEUGLUSERLEULYSVAL
5   PHELEULYSASPALAMETSERVALASNGLY
6   ARGGLUGLUALALEULYSALAGLUTYRGLU
7   LYSSERTYRLYSGLUPHEPHEASPTRPLEU
8   SERLYSASPVALASNARGGLNLYSGLUPHE
9   ILESERSERPHEASPASNILESERSERILE
10   VALSERLYSALAVALASPALASERLYSLYS
11   ARGARGPROTHRGLUGLNGLNSERLEUGLY
12   PHELYSGLUTYRVALCYSTYRLYSILELYS
13   ASNSERLYSGLYGLUALALEUSERLEUPHE
14   PHEGLNLYSVALVALASPALAPHEGLYALA
15   ASPPROTYRLYSLYSASPASNASPGLUSER
16   VALGLNLYSPROVALLYSCYSASNGLUGLU
17   ILEPHELYSVALILELYSLYSVALLEUTHR
18   GLUSERGLUSERASNASNGLULEULYSASN
19   LEULYSASNTYRGLYASNVAL

Samples:

sample_1: BBA36, [U-98% 13C; U-98% 15N], 1 ± 0.2 mM; sodium chloride 100 ± 2 mM; TRIS 20 ± 1 mM; EDTA 1 ± 0.5 mM

sample_conditions_1: ionic strength: 121 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

Poky, Manthey, Tonelli, Clos II, Rahimi, Markley and Lee - chemical shift assignment, data analysis

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

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

TopSpin, Bruker Biospin - processing

NMR spectrometers:

  • Bruker Bruker Ascend 700 MHz

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