BMRB Entry 19458

Title:
CR1-2-3
Deposition date:
2013-08-27
Original release date:
2013-11-11
Authors:
Park, Hyon; Guariento, Mara; Maciejewski, Mateusz; Hauart, Richard; Tham, Wai-Hong; Cowman, Alan; Schmidt, Christoph; Martens, Haydyn; Liszewski, Kathryn; Hourcade, Dennis; Barlow, Paul; Atkinson, John
Citation:

Citation: Park, Hyon Ju; Guariento, Mara; Maciejewski, Mateusz; Hauhart, Richard; Tham, Wai-Hong; Cowman, Alan; Schmidt, Christoph; Mertens, Haydyn; Liszewski, M. Kathryn; Hourcade, Dennis; Barlow, Paul; Atkinson, John. "Using Mutagenesis and Structural Biology to Map the Binding Site for the Plasmodium falciparum Merozoite Protein PfRh4 on the Human Immune Adherence Receptor."  J. Biol. Chem. 289, 450-463 (2014).
PubMed: 24214979

Assembly members:

Assembly members:
CR1_2-3, polymer, 136 residues, 14275.196 Da.

Natural source:

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Pichia pastoris   Vector: pPICZaB

Data sets:
Data typeCount
13C chemical shifts152
15N chemical shifts67
1H chemical shifts267

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Recombinant CR1 fragment, domains 2-31

Entities:

Entity 1, Recombinant CR1 fragment, domains 2-3 136 residues - 14275.196 Da.

1   GLUALAGLUALALYSSERCYSARGASNPRO
2   PROASPPROVALASNGLYMETVALHISVAL
3   ILELYSGLYILEGLNPHEGLYSERGLNILE
4   LYSTYRSERCYSTHRLYSGLYTYRARGLEU
5   ILEGLYSERSERSERALATHRCYSILEILE
6   SERGLYASPTHRVALILETRPASPTHRGLU
7   THRPROILECYSASPARGILEPROCYSGLY
8   LEUPROPROTHRILETHRASNGLYASPPHE
9   ILESERTHRASNARGGLUASNPHEHISTYR
10   GLYSERVALVALTHRTYRARGCYSASNPRO
11   GLYSERGLYGLYARGLYSVALPHEGLULEU
12   VALGLYGLUPROSERILETYRCYSTHRSER
13   ASNASPASPGLNVALGLYILETRPSERGLY
14   PROALAPROGLNCYSILE

Samples:

sample_1: CR1 2-3, [U-99% 13C; U-99% 15N], 0.8 mM; sodium phosphate 10 mM; H2O 90%; D2O 10%

sample_2: CR1 2-3, [U-99% 13C; U-99% 15N], 0.8 mM; sodium phosphate 10 mM; D2O 100%

sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

AZARA, Boucher - processing

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

ANALYSIS, CCPN - chemical shift assignment, peak picking

ProcheckNMR, Laskowski and MacArthur - Quality assessment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB

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