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 17557

Title: Solution structure of the dimerization domain of human ribosomal protein P1/P2 heterodimer   PubMed: 22135285

Deposition date: 2011-03-30 Original release date: 2011-12-14

Authors: Lee, Ka-Ming; Yu, Conny Wing-Heng; Chiu, Teddy Yu-Hin; Sze, Kong-Hung; Shaw, Pang-Chui; Wong, Kam-Bo

Citation: Lee, Ka-Ming; Yu, Conny Wing-Heng; Chiu, Teddy Yu-Hin; Sze, Kong-Hung; Shaw, Pang-Chui; Wong, Kam-Bo. "Solution structure of the dimerization domain of the eukaryotic stalk P1/P2 complex reveals the structural organization of eukaryotic stalk complex."  Nucleic Acids Res. 40, 3172-3182 (2012).

Assembly members:
entity_1, polymer, 69 residues, 7088.202 Da.
entity_2, polymer, 70 residues, 7207.247 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):
entity_1: MASVSELACIYSALILHDDE VTVTEDKINALIKAAGVNVE PFWPGLFAKALANVNIGSLI CNVGAGGPA
entity_2: AMRYVASYLLAALGGNSSPS AKDIKKILDSVGIEADDDRL NKVISELNGKNIEDVIAQGI GKLASVPAGG

Data sets:
Data typeCount
13C chemical shifts401
1H chemical shifts801

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 69 residues - 7088.202 Da.

1   METALASERVALSERGLULEUALACYSILE
2   TYRSERALALEUILELEUHISASPASPGLU
3   VALTHRVALTHRGLUASPLYSILEASNALA
4   LEUILELYSALAALAGLYVALASNVALGLU
5   PROPHETRPPROGLYLEUPHEALALYSALA
6   LEUALAASNVALASNILEGLYSERLEUILE
7   CYSASNVALGLYALAGLYGLYPROALA

Entity 2, entity_2 70 residues - 7207.247 Da.

1   ALAMETARGTYRVALALASERTYRLEULEU
2   ALAALALEUGLYGLYASNSERSERPROSER
3   ALALYSASPILELYSLYSILELEUASPSER
4   VALGLYILEGLUALAASPASPASPARGLEU
5   ASNLYSVALILESERGLULEUASNGLYLYS
6   ASNILEGLUASPVALILEALAGLNGLYILE
7   GLYLYSLEUALASERVALPROALAGLYGLY

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 1 mM; entity_2, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

ARIA, Brunger, Adams, Clore, Gros, Nilges and Read, Linge, O, . - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 19086 15997 19086
PDB
DBJ BAB25292 BAB27095 BAB79474 BAC40128 BAE41097 BAB22086 BAB25616 BAB27066 BAB28217 BAB79475
EMBL CAA33200 CAG29335 CAG47005 CAG47008 CAG47044
GB AAA36471 AAA70106 AAH03369 AAH07590 AAH58151 AAA36472 AAC48755 AAH05354 AAH05920 AAH07573
PRF 1718187B
REF NP_000994 NP_001007605 NP_001020511 NP_001123436 NP_001180503 NP_000995 NP_001078905 NP_001180505 NP_001231795 NP_001270094
SP A1XQU7 P05386 P19944 P47955 Q56K14 P05387 P19943 P42899 P99027 Q6X9Z5
TPG DAA21200 DAA25760 DAA13527