BMRB Entry 18517

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18517
MolProbity Validation Chart

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Title:
Solution structure of EDK-delta-Bd37 from Babesia divergens
Deposition date:
2012-06-12
Original release date:
2012-08-29
Authors:
Murciano, Brice; Barthe, Philippe; Delbecq, Stephane; Roumestand, Christian
Citation:

Citation: Barthe, Philippe; Murciano, Brice; Schetters, Theo; Gorenflot, Andre; Delbecq, Stephane; Roumestand, Christian. "1H, 15N and 13C Backbone resonance assignments of a conformational mutant of the adhesion protein delta-Bd37 from Babesia divergens."  Biomol. NMR Assignments 7, 241-244 (2013).
PubMed: 22899250

Assembly members:

Assembly members:
EDK-delta-Bd37, polymer, 224 residues, 24575.496 Da.

Natural source:

Natural source:   Common Name: Apicomplexans   Taxonomy ID: 32595   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Babesia divergens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pIVEX 2.4.a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
EDK-delta-Bd37: VKTLDVLRGELRGQREAFLS EIIKSDGPFTILQLVGYLRV VDTDLLLKVDSTKVDEAGKK VKAYLEKIGIRGDSVEAALD NLMIKVYEITKGTVESSAQG TDSEELKTLLLKFSEDLKAE QELHSEAKGGEALLSSMKTQ HDELLKKFAALTPTFLTSED ISGYLTVPEYGAPMNAAKWA KVEGMIHGKLESSEVPANLK ALVAELIELRAQMMALLYGP IGHH

Data sets:
Data typeCount
13C chemical shifts693
15N chemical shifts208
1H chemical shifts1510

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1EDK-delta-Bd371

Entities:

Entity 1, EDK-delta-Bd37 224 residues - 24575.496 Da.

1   VALLYSTHRLEUASPVALLEUARGGLYGLU
2   LEUARGGLYGLNARGGLUALAPHELEUSER
3   GLUILEILELYSSERASPGLYPROPHETHR
4   ILELEUGLNLEUVALGLYTYRLEUARGVAL
5   VALASPTHRASPLEULEULEULYSVALASP
6   SERTHRLYSVALASPGLUALAGLYLYSLYS
7   VALLYSALATYRLEUGLULYSILEGLYILE
8   ARGGLYASPSERVALGLUALAALALEUASP
9   ASNLEUMETILELYSVALTYRGLUILETHR
10   LYSGLYTHRVALGLUSERSERALAGLNGLY
11   THRASPSERGLUGLULEULYSTHRLEULEU
12   LEULYSPHESERGLUASPLEULYSALAGLU
13   GLNGLULEUHISSERGLUALALYSGLYGLY
14   GLUALALEULEUSERSERMETLYSTHRGLN
15   HISASPGLULEULEULYSLYSPHEALAALA
16   LEUTHRPROTHRPHELEUTHRSERGLUASP
17   ILESERGLYTYRLEUTHRVALPROGLUTYR
18   GLYALAPROMETASNALAALALYSTRPALA
19   LYSVALGLUGLYMETILEHISGLYLYSLEU
20   GLUSERSERGLUVALPROALAASNLEULYS
21   ALALEUVALALAGLULEUILEGLULEUARG
22   ALAGLNMETMETALALEULEUTYRGLYPRO
23   ILEGLYHISHIS

Samples:

sample_1: EDK-delta-Bd37, [U-100% 15N], 0.45 ± 0.01 mM; H2O, [U-100% 15N], 90%; D2O, [U-100% 15N], 10%

sample_2: EDK-delta-Bd37, [U-100% 13C; U-100% 15N], 0.38 ± 0.01 mM; H2O, [U-100% 15N], 90%; D2O, [U-100% 15N], 10%

sample_conditions_1: ionic strength: 50 mM; pH: 6.9; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HCACOsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1

Software:

GIFA v4.44, Delsuc - processing

CINDY v1.8, Padilla - data analysis

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 500 MHz

Related Database Links:

BMRB 15158
PDB
EMBL CAD19563 CAD48924

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