BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15158

Title: Solution structure of the adhesion protein Bd37 from Babesia divergens   PubMed: 18035372

Authors: Auguin, Daniel; Yang, Yin-Shan; Lohr, Frank; Arold, Stefan; Schetters, Theo; Precigout, Eric; Gorenflot, Andre; Delbecq, Stephane; Roumestand, Christian

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).

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

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

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

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

Data sets:
  • assigned_chemical_shifts
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 2JO7 2LUD
EMBL CAD19563 CAD48924