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 25449

Title: Solution structure of RNA recognition motif of a cyclophilin33 - like protein from Plasmodium falciparum

Deposition date: 2015-01-22 Original release date: 2016-01-25

Authors: Ganguly, Akshay Kumar; Bhavesh, Neel Sarovar

Citation: Ganguly, Akshay Kumar; Bhavesh, Neel Sarovar. "Solution structure of RNA recognition motif of a cyclophilin33 - like protein from Plasmodium falciparum"  Not known ., .-..

Assembly members:
RRM, polymer, 89 residues, 10149.340 Da.

Natural source:   Common Name: Malaria   Taxonomy ID: 36329   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Plasmodium falciparum

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

Entity Sequences (FASTA):
RRM: GSHMSDNNATDILFVGGIDE TIDEKSLYDIFSSFGDIRNI EVPLNMTTKKNRGFAFVEYV EVDDAKHALYNMNNFELNGK RIHVNYSKT

Data sets:
Data typeCount
13C chemical shifts366
15N chemical shifts97
1H chemical shifts535

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RRM1

Entities:

Entity 1, RRM 89 residues - 10149.340 Da.

Residues G,S and H at the N-terminus are part of a non-native affinity tag from the vector pET28a and have been renumbered to -2,-1 and 0.

1   GLYSERHISMETSERASPASNASNALATHR
2   ASPILELEUPHEVALGLYGLYILEASPGLU
3   THRILEASPGLULYSSERLEUTYRASPILE
4   PHESERSERPHEGLYASPILEARGASNILE
5   GLUVALPROLEUASNMETTHRTHRLYSLYS
6   ASNARGGLYPHEALAPHEVALGLUTYRVAL
7   GLUVALASPASPALALYSHISALALEUTYR
8   ASNMETASNASNPHEGLULEUASNGLYLYS
9   ARGILEHISVALASNTYRSERLYSTHR

Samples:

sample_1: RRM, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DSS 50 uM; D2O 10%; H2O 90%

sample_2: RRM, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DSS 50 uM; D2O 100%

sample_conditions_1: ionic strength: 20 mM; pH: 6.8; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_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
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 700 MHz

Related Database Links:

NCBI XP_002809024.1

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