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 6249

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for BD37

Deposition date: 2004-06-23 Original release date: 2005-02-08

Authors: Yang, Yin-Shan; Delbecq, Stephane; Roumestand, Christian

Citation: Yang, Yin-Shan; Delbecq, Stephane; Strub, Marie-Paule; Lohr, Frank; Schetters, Theo; Gorenflot, Andre; Precigout, Eric; Roumestand, Christian. "Letter to the Editor: 1H, 15N and 13C Backbone resonance assignments of the 37 kDA surface antigen protein Bd37 from Babesia divergens."  J. Biomol. NMR 31, 67-68 (2005).

Assembly members:
BD37, polymer, 294 residues, 37000 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

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
1H chemical shifts557
15N chemical shifts278
13C chemical shifts829

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 - 37000 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-95% 13C; U90% 15N; U80% 2H], 0.8 – 0.1 mM; Sodium Phosphate10 – 1 mM; Sodium Chloride50 – 5 mM

Ex-cond_1: pH: 6.8; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
not availablesample_1not availableEx-cond_1

Software:

GIFA v4 -

NMR spectrometers:

  • BRUKER AVANCE 600 MHz
  • BRUKER AVANCE 800 MHz

Related Database Links:

BMRB 15158 18517
PDB
EMBL CAD19563 CAD48924

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts