BMRB Entry 25266

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25266
MolProbity Validation Chart

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Title:
Solution structure of decorin binding protein B from Borrelia burgdorferi
Deposition date:
2014-10-03
Original release date:
2015-08-17
Authors:
Wang, Xu; Feng, Wei
Citation:

Citation: Wang, Xu; Feng, Wei; Chao, Alex. "Structure of Decorin Binding Protein B from Borrelia Spirochetes"  .

Assembly members:

Assembly members:
DBPB, polymer, 167 residues, 36406.660 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
DBPB: SSIGLVERTNAALESSSKDL KNKILKIKKEATGKGVLFEA FTGLKTGSKVTSGGLALREA KVQAIVETGKFLKIIEEEAL KLKETGNSGQFLAMFDLMLE VVESLEDVGIIGLKARVLEE SKNNPINTAERLLAAKAQIE NQLKVVKEKQNIENGGEKKN NKSKKKK

Data sets:
Data typeCount
13C chemical shifts711
15N chemical shifts173
1H chemical shifts1004

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 167 residues - 36406.660 Da.

1   SERSERILEGLYLEUVALGLUARGTHRASN
2   ALAALALEUGLUSERSERSERLYSASPLEU
3   LYSASNLYSILELEULYSILELYSLYSGLU
4   ALATHRGLYLYSGLYVALLEUPHEGLUALA
5   PHETHRGLYLEULYSTHRGLYSERLYSVAL
6   THRSERGLYGLYLEUALALEUARGGLUALA
7   LYSVALGLNALAILEVALGLUTHRGLYLYS
8   PHELEULYSILEILEGLUGLUGLUALALEU
9   LYSLEULYSGLUTHRGLYASNSERGLYGLN
10   PHELEUALAMETPHEASPLEUMETLEUGLU
11   VALVALGLUSERLEUGLUASPVALGLYILE
12   ILEGLYLEULYSALAARGVALLEUGLUGLU
13   SERLYSASNASNPROILEASNTHRALAGLU
14   ARGLEULEUALAALALYSALAGLNILEGLU
15   ASNGLNLEULYSVALVALLYSGLULYSGLN
16   ASNILEGLUASNGLYGLYGLULYSLYSASN
17   ASNLYSSERLYSLYSLYSLYS

Samples:

sample: DBPB, [U-100% 13C; U-100% 15N], 0.8 mM; sodium phosphate 50 mM; sodium chloride 150 mM; H2O 95%; D2O 5%

sample_conditions: ionic strength: 0.2 M; pH: 5.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsampleisotropicsample_conditions
2D 1H-15N HSQCsampleisotropicsample_conditions
3D 1H-13C NOESY aliphaticsampleisotropicsample_conditions
3D HNCACBsampleisotropicsample_conditions
3D CBCA(CO)NHsampleisotropicsample_conditions
3D H(CCO)NHsampleisotropicsample_conditions
3D C(CO)NHsampleisotropicsample_conditions
3D 1H-13C NOESYsampleisotropicsample_conditions
3D 1H-15N NOESYsampleisotropicsample_conditions

Software:

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

NMRView, Johnson, One Moon Scientific - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
GB AAC18819 AAC18824 AAC66244 AAC70021 AAC70023
REF NP_045698 WP_010258353 WP_010890381 WP_012666179 WP_012672539
SP C6C2E5 P0CL68
AlphaFold C6C2E5 P0CL68

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