BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 18329

Title: Structure of decorbin-binding protein A from Borrelia burgdorferi   PubMed: 22985470

Authors: Wang, Xu

Citation: Wang, Xu. "Solution structure of decorin-binding protein A from Borrelia burgdorferi"  Biochemistry 51, 8353-8362 (2012).

Assembly members:
DBPA, polymer, 336 residues, 37092.648 Da.

Natural source:   Common Name: Borrelia burgdorferi str. B31   Taxonomy ID: 224326   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Borrelia burgdorferi

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

Entity Sequences (FASTA):
DBPA: SAGLTGATKIRLERSAKDIT DEIDAIKKDAALKGVNFDAF KDKKTGSGVSENPFILEAKV RATTVAEKFVIAIEEEATKL KETGSSGEFSAMYDLMFEVS KPLQKLGIQEMTKTVSDAAE ENPPTTAQGVLEIAKKMREK LQRVHTKNYCTLKKKENSTF TDEKCKNNSAGLTGATKIRL ERSAKDITDEIDAIKKDAAL KGVNFDAFKDKKTGSGVSEN PFILEAKVRATTVAEKFVIA IEEEATKLKETGSSGEFSAM YDLMFEVSKPLQKLGIQEMT KTVSDAAEENPPTTAQGVLE IAKKMREKLQRVHTKNYCTL KKKENSTFTDEKCKNN

Data sets:
Data typeCount
13C chemical shifts633
15N chemical shifts156
1H chemical shifts936
residual dipolar couplings215

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DBPA1

Entities:

Entity 1, DBPA 336 residues - 37092.648 Da.

residue 24 to 191 of the protein decorin-binding protein A from Borrelia burgdorferi strain B31

1   SERALAGLYLEUTHRGLYALATHRLYSILE
2   ARGLEUGLUARGSERALALYSASPILETHR
3   ASPGLUILEASPALAILELYSLYSASPALA
4   ALALEULYSGLYVALASNPHEASPALAPHE
5   LYSASPLYSLYSTHRGLYSERGLYVALSER
6   GLUASNPROPHEILELEUGLUALALYSVAL
7   ARGALATHRTHRVALALAGLULYSPHEVAL
8   ILEALAILEGLUGLUGLUALATHRLYSLEU
9   LYSGLUTHRGLYSERSERGLYGLUPHESER
10   ALAMETTYRASPLEUMETPHEGLUVALSER
11   LYSPROLEUGLNLYSLEUGLYILEGLNGLU
12   METTHRLYSTHRVALSERASPALAALAGLU
13   GLUASNPROPROTHRTHRALAGLNGLYVAL
14   LEUGLUILEALALYSLYSMETARGGLULYS
15   LEUGLNARGVALHISTHRLYSASNTYRCYS
16   THRLEULYSLYSLYSGLUASNSERTHRPHE
17   THRASPGLULYSCYSLYSASNASNSERALA
18   GLYLEUTHRGLYALATHRLYSILEARGLEU
19   GLUARGSERALALYSASPILETHRASPGLU
20   ILEASPALAILELYSLYSASPALAALALEU
21   LYSGLYVALASNPHEASPALAPHELYSASP
22   LYSLYSTHRGLYSERGLYVALSERGLUASN
23   PROPHEILELEUGLUALALYSVALARGALA
24   THRTHRVALALAGLULYSPHEVALILEALA
25   ILEGLUGLUGLUALATHRLYSLEULYSGLU
26   THRGLYSERSERGLYGLUPHESERALAMET
27   TYRASPLEUMETPHEGLUVALSERLYSPRO
28   LEUGLNLYSLEUGLYILEGLNGLUMETTHR
29   LYSTHRVALSERASPALAALAGLUGLUASN
30   PROPROTHRTHRALAGLNGLYVALLEUGLU
31   ILEALALYSLYSMETARGGLULYSLEUGLN
32   ARGVALHISTHRLYSASNTYRCYSTHRLEU
33   LYSLYSLYSGLUASNSERTHRPHETHRASP
34   GLULYSCYSLYSASNASN

Samples:

sample_1: DBPA, [U-100% 13C; U-100% 15N], 0.8 mM; sodium phosphate 50 mM; D2O 10%; H2O 90%

gel_sample: DBPA, [U-100% 13C; U-100% 15N], 0.8 mM; sodium phosphate 50 mM; D2O 10%; H2O 90%; polyacrylamide 5%

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
J-modulated 15N HSQCgel_sampleanisotropicsample_conditions_1
JNC-modulated 15N HSQCgel_sampleanisotropicsample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - data analysis

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Agilent Inova 800 800 MHz

Related Database Links:

PDB
EMBL CAG38080 CAG38331 CAG38379 CAG38382 CAG38384
GB AAC66250 AAC70047 AAC70053 AAC70064 AAL35357
REF NP_045697 WP_010890380 YP_009075678
SP O50917