BMRB Entry 17633

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17633
MolProbity Validation Chart

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Title:
NMR structure of BC28.1
Deposition date:
2011-05-09
Original release date:
2012-02-03
Authors:
Roumestand, Christian; Delbecq, Stephane; Yang, Yin-Shan
Citation:

Citation: Yang, Yin-Shan; Murciano, Brice; Moubri, Karina; Cibrelus, Prisca; Schetters, Theo; Gorenflot, Andre; Delbecq, Stephane; Roumestand, Christian. "Structural and Functional Characterization of Bc28.1, Major Erythrocyte-binding Protein from Babesia canis Merozoite Surface."  J. Biol. Chem. 287, 9495-9508 (2012).
PubMed: 22294693

Assembly members:

Assembly members:
BC28.1, polymer, 223 residues, 24947.393 Da.

Natural source:

Natural source:   Common Name: Babesia canis   Taxonomy ID: 5867   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Babesia canis

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BC28.1: SSGIEGCTEDEKRDSVVEGA TSVEASLKEQIDWLAERYSA DLTNKDTSKWNTDEKVKELL NEKAVGIESRLLAIAKEFHK LKSVLCTGVNETPAHVANRV SPGDAISMLYVLSITHRELS SLKNKIDEWKKVKASEDGTK VIQNIKDDRTNTWFVAHGFK VAELNDVTLEKLATVVNELV SHKDMIYINDAMKQNVDKWT KEESERLAMMAEQGISGAKG KKD

Data sets:
Data typeCount
13C chemical shifts671
15N chemical shifts224
1H chemical shifts1457

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1BC28.11

Entities:

Entity 1, BC28.1 223 residues - 24947.393 Da.

1   SERSERGLYILEGLUGLYCYSTHRGLUASP
2   GLULYSARGASPSERVALVALGLUGLYALA
3   THRSERVALGLUALASERLEULYSGLUGLN
4   ILEASPTRPLEUALAGLUARGTYRSERALA
5   ASPLEUTHRASNLYSASPTHRSERLYSTRP
6   ASNTHRASPGLULYSVALLYSGLULEULEU
7   ASNGLULYSALAVALGLYILEGLUSERARG
8   LEULEUALAILEALALYSGLUPHEHISLYS
9   LEULYSSERVALLEUCYSTHRGLYVALASN
10   GLUTHRPROALAHISVALALAASNARGVAL
11   SERPROGLYASPALAILESERMETLEUTYR
12   VALLEUSERILETHRHISARGGLULEUSER
13   SERLEULYSASNLYSILEASPGLUTRPLYS
14   LYSVALLYSALASERGLUASPGLYTHRLYS
15   VALILEGLNASNILELYSASPASPARGTHR
16   ASNTHRTRPPHEVALALAHISGLYPHELYS
17   VALALAGLULEUASNASPVALTHRLEUGLU
18   LYSLEUALATHRVALVALASNGLULEUVAL
19   SERHISLYSASPMETILETYRILEASNASP
20   ALAMETLYSGLNASNVALASPLYSTRPTHR
21   LYSGLUGLUSERGLUARGLEUALAMETMET
22   ALAGLUGLNGLYILESERGLYALALYSGLY
23   LYSLYSASP

Samples:

sample_1: BC28.1, [U-15N], 0.5 ± 0.02 mM; H2O 90%; D2O 10%; Sodium phosphate 10 mM; NaCl 50 mM

sample_2: BC28.1, [U-13C; U-15N], 0.5 ± 0.02 mM; H2O 90%; D2O 10%; Sodium phosphate 10 mM; NaCl 50 mM

sample_3: BC28.1 0.1 ± 0.005 mM; D2O 100%; sodium phosphate 10 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; 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 1H-13C NOESYsample_2isotropicsample_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
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
2D 1H-1H TOCSYsample_3isotropicsample_conditions_1

Software:

GIFA v4.4, Delsuc - processing

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
  • Bruker Avance 950 MHz

Related Database Links:

PDB
GB AKN35161

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