BMRB Entry 25157

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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/BMR25157
MolProbity Validation Chart

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Title:
Strcucture of Decorin Binding Protein A from strain PBr of Borrelia garinii
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:
entity, polymer, 164 residues, 35781.660 Da.

Natural source:

Natural source:   Common Name: spirochetes   Taxonomy ID: 498743   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Borrelia garinii

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GLTGETKIRLESSAQEIKDE INKIKANAKKEGVKFEAFTN TQTGSKISEKPEFILKAKIK AIQVAERFVKAIKEEAEKLK KSGSSGAFSAMYDLMIDVSK PLEEIGIQKMTGTVKEAAQK TPATTADGIIAIAQAMEDKL NNVNKKQHDALKNLKEKAKT ATTT

Data sets:
Data typeCount
13C chemical shifts682
15N chemical shifts155
1H chemical shifts973

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 164 residues - 35781.660 Da.

1   GLYLEUTHRGLYGLUTHRLYSILEARGLEU
2   GLUSERSERALAGLNGLUILELYSASPGLU
3   ILEASNLYSILELYSALAASNALALYSLYS
4   GLUGLYVALLYSPHEGLUALAPHETHRASN
5   THRGLNTHRGLYSERLYSILESERGLULYS
6   PROGLUPHEILELEULYSALALYSILELYS
7   ALAILEGLNVALALAGLUARGPHEVALLYS
8   ALAILELYSGLUGLUALAGLULYSLEULYS
9   LYSSERGLYSERSERGLYALAPHESERALA
10   METTYRASPLEUMETILEASPVALSERLYS
11   PROLEUGLUGLUILEGLYILEGLNLYSMET
12   THRGLYTHRVALLYSGLUALAALAGLNLYS
13   THRPROALATHRTHRALAASPGLYILEILE
14   ALAILEALAGLNALAMETGLUASPLYSLEU
15   ASNASNVALASNLYSLYSGLNHISASPALA
16   LEULYSASNLEULYSGLULYSALALYSTHR
17   ALATHRTHRTHR

Samples:

sample: PBr, [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