BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 19459

Title: CR1~1-2   PubMed: 24214979

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: 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).

Assembly members:
CR1_1-2, polymer, 128 residues, 13771.797 Da.

Natural source:   Common Name: baker   Taxonomy ID: 4932   Superkingdom: not available   Kingdom: not available   Genus/species: Eukaryota Fungi

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

Entity Sequences (FASTA):
CR1_1-2: EAEAAGQCNAPEWLPFARPT QLTDEFEFPIGTYLNYECRP GYSGRPFSIICLKNSVWTGA KDRCRRKSCRNPPDPVNGMV HVIKGIQFGSQIKYSCTKGY RLIGSSSATCIISGDTVIWD QETPICDR

Data sets:
Data typeCount
13C chemical shifts518
15N chemical shifts121
1H chemical shifts731

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Recombinant CR1 fragment, domains 1-21

Entities:

Entity 1, Recombinant CR1 fragment, domains 1-2 128 residues - 13771.797 Da.

1   GLUALAGLUALAALAGLYGLNCYSASNALA
2   PROGLUTRPLEUPROPHEALAARGPROTHR
3   GLNLEUTHRASPGLUPHEGLUPHEPROILE
4   GLYTHRTYRLEUASNTYRGLUCYSARGPRO
5   GLYTYRSERGLYARGPROPHESERILEILE
6   CYSLEULYSASNSERVALTRPTHRGLYALA
7   LYSASPARGCYSARGARGLYSSERCYSARG
8   ASNPROPROASPPROVALASNGLYMETVAL
9   HISVALILELYSGLYILEGLNPHEGLYSER
10   GLNILELYSTYRSERCYSTHRLYSGLYTYR
11   ARGLEUILEGLYSERSERSERALATHRCYS
12   ILEILESERGLYASPTHRVALILETRPASP
13   GLNGLUTHRPROILECYSASPARG

Samples:

sample_1: CR1 1-2, [U-99% 13C; U-99% 15N], 0.56 mM; sodium acetate, [U-100% 2H], 20 mM; H2O 90%; D2O 10%

sample_2: CR1 1-2, [U-99% 13C; U-99% 15N], 0.56 mM; sodium acetate, [U-100% 2H], 20 mM; D2O 100%

sample_conditions_1: pH: 4; pressure: 1 atm; temperature: 310 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 HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_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
DBJ BAG60695
GB AAD15289

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts