BMRB Entry 26773

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26773

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Title:
Chemical shift assignments of Spectrin repeat a17
Deposition date:
2016-04-01
Original release date:
2017-08-01
Authors:
Cutts, Erin; Vakonakis, Ioannis
Citation:

Citation: Cutts, Erin; Laasch, Niklas; Reiter, Dirk; Trenker, Raphael; Slater, Leanne; Stansfeld, Phillip; Vakonakis, Ioannis. "Structural analysis of P. falciparum KAHRP and PfEMP1 complexes with host erythrocyte spectrin suggests a model for cytoadherent knob protrusions"  PLoS Pathog. 13, e1006552-e1006552 (2017).
PubMed: 28806784

Assembly members:

Assembly members:
a17, polymer, 126 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET16c

Entity Sequences (FASTA):

Entity Sequences (FASTA):
a17: GPGAHHEKLKEAYALFQFFQ DLDDEESWIEEKLIRVSSQD YGRDLQGVQNLLKKHKRLEG ELVAHEPAIQNVLDMAEKLK DKAAVGQEEIQLRLAQFVEH WEKLKELAKARGLKLEESLE YLQFMQ

Data sets:
Data typeCount
13C chemical shifts368
15N chemical shifts123
1H chemical shifts240

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1a171

Entities:

Entity 1, a17 126 residues - Formula weight is not available

Residues 1-3 correspond to cloning artifacts

1   GLYPROGLYALAHISHISGLULYSLEULYS
2   GLUALATYRALALEUPHEGLNPHEPHEGLN
3   ASPLEUASPASPGLUGLUSERTRPILEGLU
4   GLULYSLEUILEARGVALSERSERGLNASP
5   TYRGLYARGASPLEUGLNGLYVALGLNASN
6   LEULEULYSLYSHISLYSARGLEUGLUGLY
7   GLULEUVALALAHISGLUPROALAILEGLN
8   ASNVALLEUASPMETALAGLULYSLEULYS
9   ASPLYSALAALAVALGLYGLNGLUGLUILE
10   GLNLEUARGLEUALAGLNPHEVALGLUHIS
11   TRPGLULYSLEULYSGLULEUALALYSALA
12   ARGGLYLEULYSLEUGLUGLUSERLEUGLU
13   TYRLEUGLNPHEMETGLN

Samples:

sample_1: a17, [U-99% 13C; U-99% 15N], 0.5 mM; sodium chloride 300 mM; sodium phosphate 20 mM; DTT 1 mM; DSS 0.05 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.34 M; pH: 6.5; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

CCPN_Analysis, Prof. Geerten Vuister - data analysis

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker Avance 750 MHz

Related Database Links:

UNP P02549
AlphaFold Q6LDY5

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