BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19086

Title: Solution structure of human ribosomal protein P1.P2 heterodimer   PubMed: 23892290

Deposition date: 2013-03-12 Original release date: 2014-09-19

Authors: Lee, Kaming; Yusa, K.; Chu, L.; Yu, C.; Shaw, P.; Oono, M.; Miyoshi, T.; Ito, K.; Wong, K.; Uchiumi, T.

Citation: Lee, Ka-Ming; Yusa, Kazuyuki; Chu, Lai-On; Yu, Conny Wing-Heng; Oono, Moe; Miyoshi, Tomohiro; Ito, Kosuke; Shaw, Pang-Chui; Wong, Kam-Bo; Uchiumi, Toshio. "Solution structure of human P1.P2 heterodimer provides insights into the role of eukaryotic stalk in recruiting the ribosome-inactivating protein trichosanthin to the ribosome."  Nucleic Acids Res. 41, 8776-8787 (2013).

Assembly members:
60S_ACIDIC_RIBOSOMAL_PROTEIN_P1, polymer, 114 residues, 11480.6435 Da.
60S_ACIDIC_RIBOSOMAL_PROTEIN_P2, polymer, 116 residues, 11699.6986 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: ESCHERICHIA COLI

Entity Sequences (FASTA):
60S_ACIDIC_RIBOSOMAL_PROTEIN_P1: MASVSELACIYSALILHDDE VTVTEDKINALIKAAGVNVE PFWPGLFAKALANVNIGSLI CNVGAGGPAPAAGAAPAGGP APSTAAAPAEEKKVEAKKEE SEESDDDMGFGLFD
60S_ACIDIC_RIBOSOMAL_PROTEIN_P2: AMRYVASYLLAALGGNSSPS AKDIKKILDSVGIEADDDRL NKVISELNGKNIEDVIAQGI GKLASVPAGGAVAVSAAPGS AAPAAGSAPAAAEEKKDEKK EESEESDDDMGFGLFD

Data sets:
Data typeCount
13C chemical shifts205
1H chemical shifts632

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
160S ACIDIC RIBOSOMAL PROTEIN P11
260S ACIDIC RIBOSOMAL PROTEIN P22

Entities:

Entity 1, 60S ACIDIC RIBOSOMAL PROTEIN P1 114 residues - 11480.6435 Da.

1   METALASERVALSERGLULEUALACYSILE
2   TYRSERALALEUILELEUHISASPASPGLU
3   VALTHRVALTHRGLUASPLYSILEASNALA
4   LEUILELYSALAALAGLYVALASNVALGLU
5   PROPHETRPPROGLYLEUPHEALALYSALA
6   LEUALAASNVALASNILEGLYSERLEUILE
7   CYSASNVALGLYALAGLYGLYPROALAPRO
8   ALAALAGLYALAALAPROALAGLYGLYPRO
9   ALAPROSERTHRALAALAALAPROALAGLU
10   GLULYSLYSVALGLUALALYSLYSGLUGLU
11   SERGLUGLUSERASPASPASPMETGLYPHE
12   GLYLEUPHEASP

Entity 2, 60S ACIDIC RIBOSOMAL PROTEIN P2 116 residues - 11699.6986 Da.

1   ALAMETARGTYRVALALASERTYRLEULEU
2   ALAALALEUGLYGLYASNSERSERPROSER
3   ALALYSASPILELYSLYSILELEUASPSER
4   VALGLYILEGLUALAASPASPASPARGLEU
5   ASNLYSVALILESERGLULEUASNGLYLYS
6   ASNILEGLUASPVALILEALAGLNGLYILE
7   GLYLYSLEUALASERVALPROALAGLYGLY
8   ALAVALALAVALSERALAALAPROGLYSER
9   ALAALAPROALAALAGLYSERALAPROALA
10   ALAALAGLUGLULYSLYSASPGLULYSLYS
11   GLUGLUSERGLUGLUSERASPASPASPMET
12   GLYPHEGLYLEUPHEASP

Samples:

sample_1: 60S ACIDIC RIBOSOMAL PROTEIN P1, [U-13C; U-15N], 1 mM; 60S ACIDIC RIBOSOMAL PROTEIN P2, [U-13C; U-15N], 1 mM

sample_conditions_1: ionic strength: 150.000 mM; pH: 6.500; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

NameSampleSample stateSample conditions
NOESYsample_1solutionsample_conditions_1
TOCSYsample_1solutionsample_conditions_1
COSYsample_1solutionsample_conditions_1

Software:

AutoDep v4.3, Johnson, One Moon Scientific, PDBe - chemical shift assignment, collection

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - chemical shift assignment, collection

NMRView vany - chemical shift assignment, collection

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

UNP RLA1_HUMAN P05387