BMRB Entry 51862

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51862

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Title:
1H, 13C, and 15N chemical shift assignments of Plasmodium falciparum circumsporozoite protein's C-terminal domain
Deposition date:
2023-03-01
Original release date:
2025-05-29
Authors:
Geens, Rob; Volkov, Alexander; Tompa, Peter; Sterckx, Yann
Citation:

Citation: Geens, Rob; Volkov, Alexander; Tompa, Peter; Sterckx, Yann. "1H, 13C, and 15N chemical shift assignments of the C-terminal domain of the Plasmodium falciparum circumsporozoite protein"  n/a ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 127 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Plasmodium falciparum   Taxonomy ID: 5833   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Plasmodium falciparum

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MKNNQGNGQGHNMPNDPNRN VDENANANSAVKNNNNEEPS DKHIKEYLNKIQNSLSTEWS PCSVTCGNGIQVRIKPGSAN KPKDELDYANDIEKKICKME KCSSVFNVVNSSENLYFQSG GHHHHHH

Data sets:
Data typeCount
13C chemical shifts431
15N chemical shifts109
1H chemical shifts658

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1PfaCSP Cext1

Entities:

Entity 1, PfaCSP Cext 127 residues - Formula weight is not available

1   METLYSASNASNGLNGLYASNGLYGLNGLY
2   HISASNMETPROASNASPPROASNARGASN
3   VALASPGLUASNALAASNALAASNSERALA
4   VALLYSASNASNASNASNGLUGLUPROSER
5   ASPLYSHISILELYSGLUTYRLEUASNLYS
6   ILEGLNASNSERLEUSERTHRGLUTRPSER
7   PROCYSSERVALTHRCYSGLYASNGLYILE
8   GLNVALARGILELYSPROGLYSERALAASN
9   LYSPROLYSASPGLULEUASPTYRALAASN
10   ASPILEGLULYSLYSILECYSLYSMETGLU
11   LYSCYSSERSERVALPHEASNVALVALASN
12   SERSERGLUASNLEUTYRPHEGLNSERGLY
13   GLYHISHISHISHISHISHIS

Samples:

sample_1: PfaCSP C-terminal domain (residues 274-384), [U-13C; U-15N], 1 mM; sodium phosphate 20 mM; sodium chloride 100 mM; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 155 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D H(C)CH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_1isotropicsample_conditions_1

Software:

TOPSPIN - collection, processing

NMRPipe - processing

CCPN - chemical shift assignment, data analysis, peak picking

qMDD - processing

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

UNP P19597

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