BMRB Entry 18517

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PDB ID: 2lud
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:

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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

Related Database Links:

BMRB 15158
PDB 2JO7 2LUD
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