BMRB Entry 15158

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR15158
MolProbity Validation Chart

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Title:
Solution structure of the adhesion protein Bd37 from Babesia divergens
Deposition date:
2007-03-02
Original release date:
2008-05-06
Authors:
Auguin, Daniel; Yang, Yin-Shan; Lohr, Frank; Arold, Stefan; Schetters, Theo; Precigout, Eric; Gorenflot, Andre; Delbecq, Stephane; Roumestand, Christian
Citation:

Citation: Delbecq, Stephane; Auguin, Daniel; Yang, Yin-Shan; Lohr, Frank; Arold, Stefan; Schetters, Theo; Precigout, Eric; Gorenflot, Andre; Roumestand, Christian. "The solution structure of the adhesion protein Bd37 from Babesia divergens reveals structural homology with eukaryotic proteins involved in membrane trafficking"  J. Mol. Biol. 375, 409-424 (2008).
PubMed: 18035372

Assembly members:

Assembly members:
Bd37, polymer, 294 residues, 31467.693 Da.

Natural source:

Natural source:   Common Name: Babesia Divergens   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 2.3MCS

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Bd37: CTNLNGSQEPAAANPVVSTP GNDAQQAGTQQGGANSKSVP EQQPQQAAGETTATVVVKTL DVLRGELRGQREAFLSEIIK SDGPFTILQLVGYLRVVDTD LLLKVDSTKVDEAGKKVKAY LEKIGIRGDSVEAALDNLMI KVYEITKGTVESSAQGTDSE ELKTLLLKFSEDLKAEQELH SEAKGGEALLSSMKTQHDEL LKKFAALTPTFLTSEDISGY LTVPEYGAPMNAAKWKKVEG MIHGKLESSEVPANLKALVA ELIELREQMMDLLYGPIGHH DCAAGSGQGSSKLN

Data sets:
Data typeCount
13C chemical shifts847
15N chemical shifts278
1H chemical shifts1543

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Bd371

Entities:

Entity 1, Bd37 294 residues - 31467.693 Da.

1   CYSTHRASNLEUASNGLYSERGLNGLUPRO
2   ALAALAALAASNPROVALVALSERTHRPRO
3   GLYASNASPALAGLNGLNALAGLYTHRGLN
4   GLNGLYGLYALAASNSERLYSSERVALPRO
5   GLUGLNGLNPROGLNGLNALAALAGLYGLU
6   THRTHRALATHRVALVALVALLYSTHRLEU
7   ASPVALLEUARGGLYGLULEUARGGLYGLN
8   ARGGLUALAPHELEUSERGLUILEILELYS
9   SERASPGLYPROPHETHRILELEUGLNLEU
10   VALGLYTYRLEUARGVALVALASPTHRASP
11   LEULEULEULYSVALASPSERTHRLYSVAL
12   ASPGLUALAGLYLYSLYSVALLYSALATYR
13   LEUGLULYSILEGLYILEARGGLYASPSER
14   VALGLUALAALALEUASPASNLEUMETILE
15   LYSVALTYRGLUILETHRLYSGLYTHRVAL
16   GLUSERSERALAGLNGLYTHRASPSERGLU
17   GLULEULYSTHRLEULEULEULYSPHESER
18   GLUASPLEULYSALAGLUGLNGLULEUHIS
19   SERGLUALALYSGLYGLYGLUALALEULEU
20   SERSERMETLYSTHRGLNHISASPGLULEU
21   LEULYSLYSPHEALAALALEUTHRPROTHR
22   PHELEUTHRSERGLUASPILESERGLYTYR
23   LEUTHRVALPROGLUTYRGLYALAPROMET
24   ASNALAALALYSTRPLYSLYSVALGLUGLY
25   METILEHISGLYLYSLEUGLUSERSERGLU
26   VALPROALAASNLEULYSALALEUVALALA
27   GLULEUILEGLULEUARGGLUGLNMETMET
28   ASPLEULEUTYRGLYPROILEGLYHISHIS
29   ASPCYSALAALAGLYSERGLYGLNGLYSER
30   SERLYSLEUASN

Samples:

sample_1: Bd37, [U-99% 15N], 0.5 – 1 mM; phosphate buffer 20 mM; NaCl 50 mM

sample_2: Bd37, [U-99% 13C; U-99% 15N], 0.5 – 1 mM; phosphate buffer 20 mM; NaCl 50 mM

sample_3: Bd37, [13C]-I,V,L methyl, 0.5 – 1 mM; phosphate buffer 20 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 310 K

sample_conditions_2: pD: 6.8

sample_conditions_3: pH: 6.8

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1anisotropicsample_conditions_1
3D 1H-15N NOESYsample_1anisotropicsample_conditions_1
3D 1H-13C NOESYsample_2anisotropicsample_conditions_2
3D 1H-15N NOESYsample_1anisotropicsample_conditions_2
(in-phase/antiphase) [15N-1H] HSQCsample_1isotropicsample_conditions_3

Software:

PREDITOR v1, (PREDITOR) Berjanskii - geometry optimization

CINDY, PADILLA - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER v8, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Koll - refinement

GIFA v4, Delsuc - processing

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 18517
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