BMRB Entry 50751

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50751

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Title:
Resonance assignment of Decorin binding protein A from European species Borrelia afzelii
Deposition date:
2021-02-08
Original release date:
2021-08-10
Authors:
Hejduk, Libor; Rathner, Adriana; Rathner, Petr; Strnad, Martin; Grubhoffer, Libor; Sterba, Jan; Rego, Ryan; Muller, Norbert
Citation:

Citation: Hejduk, Libor; Rathner, Petr; Strnad, Martin; Grubhoffer, Libor; Sterba, Jan; Rego, Ryan; Muller, Norbert; Rathner, Adriana. "Resonance assignment and secondary structure of DbpA protein from the European species, Borrelia afzelii"  Biomol. NMR Assignments 15, 415-420 (2021).
PubMed: 34357583

Assembly members:

Assembly members:
entity_1, polymer, 157 residues, 17054 Da.

Natural source:

Natural source:   Common Name: Borrelia afzelii   Taxonomy ID: 29518   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Borrelia afzelii

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pQE30

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: HHHHHHGSSLTGKARLESSV KDITNEIEKAIKEAEDAGVK TDAFTETQTGGKVGGSQIRA AKIRVADLTIKFLEATEEET ITFKENGAGEEDFSGIYDLI LNAAKAVEKIGMQGMKQAVE EAAKEKPKTTADGIIAIVKV MKAKVENIKEKQTKNQK

Data sets:
Data typeCount
13C chemical shifts450
15N chemical shifts142
1H chemical shifts915

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DbpA1

Entities:

Entity 1, DbpA 157 residues - 17054 Da.

1   HISHISHISHISHISHISGLYSERSERLEU
2   THRGLYLYSALAARGLEUGLUSERSERVAL
3   LYSASPILETHRASNGLUILEGLULYSALA
4   ILELYSGLUALAGLUASPALAGLYVALLYS
5   THRASPALAPHETHRGLUTHRGLNTHRGLY
6   GLYLYSVALGLYGLYSERGLNILEARGALA
7   ALALYSILEARGVALALAASPLEUTHRILE
8   LYSPHELEUGLUALATHRGLUGLUGLUTHR
9   ILETHRPHELYSGLUASNGLYALAGLYGLU
10   GLUASPPHESERGLYILETYRASPLEUILE
11   LEUASNALAALALYSALAVALGLULYSILE
12   GLYMETGLNGLYMETLYSGLNALAVALGLU
13   GLUALAALALYSGLULYSPROLYSTHRTHR
14   ALAASPGLYILEILEALAILEVALLYSVAL
15   METLYSALALYSVALGLUASNILELYSGLU
16   LYSGLNTHRLYSASNGLNLYS

Samples:

sample_1: potassium phosphate 20 mM; H2O 90%; D2O, [U-99% 2H], 10%; DbpA, [U-98% 13C; U-98% 15N], 470 uM

sample_conditions_1: ionic strength: 0.18 mM; pH: 6.0; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1

Software:

CARA v1.8.4.2 - chemical shift assignment

TOPSPIN v3.6.1 - collection, processing

NMR spectrometers:

  • Bruker AVANCE III 700 MHz

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