BMRB Entry 25156

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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/BMR25156
MolProbity Validation Chart

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Title:
Structure of decorin binding protein A from strain N40 of Borrelia burgdorferi
Deposition date:
2014-08-16
Original release date:
2015-03-23
Authors:
Wang, Xu; Morgan, Ashli
Citation:

Citation: Wang, Xu; Morgan, Ashli. "Structural Mechanisms Underlying Sequence-Dependent Variations in GAG Affinities of Decorin Binding Protein A, a Borrelia burgdorferi Adhesin"  Biochem. J. 467, 439-451 (2015).
PubMed: 25695518

Assembly members:

Assembly members:
DBPA, polymer, 166 residues, 36566.016 Da.

Natural source:

Natural source:   Common Name: Lime Disease causing bacterium   Taxonomy ID: 521007   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):
DBPA: GLKGETKIILERSAKDITDE INKIKKDAADNNVNFAAFTD SETGSKVSENSFILEAKVRA TTVAEKFVTAIEGEATKLKK TGSSGEFSAMYNMMLEVSGP LEELGVLRMTKTVTDAAEQH PTTTAEGILEIAKIMKTKLQ RVHTKNYCALEKKKNPNFTD EKCKNN

Data sets:
Data typeCount
13C chemical shifts427
15N chemical shifts156
1H chemical shifts663

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1DBPA1

Entities:

Entity 1, DBPA 166 residues - 36566.016 Da.

disulfide bond between C176 and C191

1   GLYLEULYSGLYGLUTHRLYSILEILELEU
2   GLUARGSERALALYSASPILETHRASPGLU
3   ILEASNLYSILELYSLYSASPALAALAASP
4   ASNASNVALASNPHEALAALAPHETHRASP
5   SERGLUTHRGLYSERLYSVALSERGLUASN
6   SERPHEILELEUGLUALALYSVALARGALA
7   THRTHRVALALAGLULYSPHEVALTHRALA
8   ILEGLUGLYGLUALATHRLYSLEULYSLYS
9   THRGLYSERSERGLYGLUPHESERALAMET
10   TYRASNMETMETLEUGLUVALSERGLYPRO
11   LEUGLUGLULEUGLYVALLEUARGMETTHR
12   LYSTHRVALTHRASPALAALAGLUGLNHIS
13   PROTHRTHRTHRALAGLUGLYILELEUGLU
14   ILEALALYSILEMETLYSTHRLYSLEUGLN
15   ARGVALHISTHRLYSASNTYRCYSALALEU
16   GLULYSLYSLYSASNPROASNPHETHRASP
17   GLULYSCYSLYSASNASN

Samples:

sample: DBPA, [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

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