BMRB Entry 51960

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51960
MolProbity Validation Chart

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Title:
1H, 13C and 15N backbone and side-chain resonance assignments of BMSA1
Deposition date:
2023-05-11
Original release date:
2023-08-30
Authors:
Mouhand, Assia; Pissarra, Joana; Delbecq, Stephane; Roumestand, Christian; Barthe, Philippe
Citation:

Citation: Mouhand, Assia; Pissarra, Joana; Delbecq, Stephane; Roumestand, Christian; Barthe, Philippe. "1H, 13C and 15N backbone and side-chain resonance assignments of BmSA1, the surface antigen of Babesia microti"  Biomol. NMR Assign. 17, 217-221 (2023).
PubMed: 37452919

Assembly members:

Assembly members:
entity_1, polymer, 254 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Babesia microti   Taxonomy ID: 5868   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Babesia microti

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pDB-his-TEV

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GHMQPNNESKKKAVKLDLDL MKETKNVCTTVNTKLVGKAK SKLNKLEGESHKEYVAEKTK EIDEKNKKFNENLVKIEKRK KIKVPADTGAEVDAVDDGVA GALSDLSSDISAIKTLTDDV SEKVSENLKDDEASATEHTD IKEKATLLQESCNGIGTILD KLAEYLNNDTTQNIKKEFDE RKKNLTSLKTKVENKDEDYV THFRDMATEAQNAVGEVKKA IDAVVAHRKAENLDVDDTLF SNLSTLLDTIIETS

Data sets:
Data typeCount
13C chemical shifts748
15N chemical shifts272
1H chemical shifts1714

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1BmSA11

Entities:

Entity 1, BmSA1 254 residues - Formula weight is not available

1   GLYHISMETGLNPROASNASNGLUSERLYS
2   LYSLYSALAVALLYSLEUASPLEUASPLEU
3   METLYSGLUTHRLYSASNVALCYSTHRTHR
4   VALASNTHRLYSLEUVALGLYLYSALALYS
5   SERLYSLEUASNLYSLEUGLUGLYGLUSER
6   HISLYSGLUTYRVALALAGLULYSTHRLYS
7   GLUILEASPGLULYSASNLYSLYSPHEASN
8   GLUASNLEUVALLYSILEGLULYSARGLYS
9   LYSILELYSVALPROALAASPTHRGLYALA
10   GLUVALASPALAVALASPASPGLYVALALA
11   GLYALALEUSERASPLEUSERSERASPILE
12   SERALAILELYSTHRLEUTHRASPASPVAL
13   SERGLULYSVALSERGLUASNLEULYSASP
14   ASPGLUALASERALATHRGLUHISTHRASP
15   ILELYSGLULYSALATHRLEULEUGLNGLU
16   SERCYSASNGLYILEGLYTHRILELEUASP
17   LYSLEUALAGLUTYRLEUASNASNASPTHR
18   THRGLNASNILELYSLYSGLUPHEASPGLU
19   ARGLYSLYSASNLEUTHRSERLEULYSTHR
20   LYSVALGLUASNLYSASPGLUASPTYRVAL
21   THRHISPHEARGASPMETALATHRGLUALA
22   GLNASNALAVALGLYGLUVALLYSLYSALA
23   ILEASPALAVALVALALAHISARGLYSALA
24   GLUASNLEUASPVALASPASPTHRLEUPHE
25   SERASNLEUSERTHRLEULEUASPTHRILE
26   ILEGLUTHRSER

Samples:

sample_1: BmSA1, [U-100% 15N], 0.9 mM; sodium phosphate 20 mM; sodium chloride 50 mM

sample_2: BmSA1, [U-100% 13C; U-100% 15N], 0.6 mM; sodium phosphate 20 mM; sodium chloride 50 mM

sample_3: BmSA1, [U-100% 15N], 0.9 mM; sodium phosphate 20 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.2; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HN(CO)CAsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HN(CA)COsample_3isotropicsample_conditions_1

Software:

CINDY v2.1 - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

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