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 11541

Title: Solution Structure of Protein-RNA Complex

Deposition date: 2013-11-12 Original release date: 2014-08-11

Authors: Takahashi, Mari; Kuwasako, Kanako; Unzai, Satoru; Tsuda, Kengo; Yoshikawa, Seiko; He, Fahu; Kobayashi, Naohiro; Guntert, Peter; Shirouzu, Mikako; Ito, Takuhiro; Tanaka, Akiko; Yokoyama, Shigeyuki; Hagiwara, Masatoshi; Kuroyanagi, Hidehito; Muto, Yutaka

Citation: Kuwasako, Kanako; Takahashi, Mari; Unzai, Satoru; Tsuda, Kengo; Yoshikawa, Seiko; He, Fahu; Kobayashi, Naohiro; Guntert, Peter; Shirouzu, Mikako; Ito, Takuhiro; Tanaka, Akiko; Yokoyama, Shigeyuki; Hagiwara, Masatoshi; Kuroyanagi, Hidehito; Muto, Yutaka. "Solution Structure of Protein-RNA Complex"  .

Assembly members:
entity_1, polymer, 103 residues, 11426.872 Da.
RNA, polymer, 6 residues, Formula weight is not available

Natural source:   Common Name: nematode   Taxonomy ID: 6239   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Caenorhabditis elegans

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: PET-15B

Entity Sequences (FASTA):
entity_1: GSTNAEPVVGSRDTMFTKIF VGGLPYHTSDKTLHEYFEQF GDIEEAVVITDRNTQKSRGY GFVTMKDRASAERACKDPNP IIDGRKANVNLAYLGAKPRT NVQ
RNA: GUGUGC

Data sets:
Data typeCount
13C chemical shifts317
15N chemical shifts97
1H chemical shifts628

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2RNA2

Entities:

Entity 1, entity_1 103 residues - 11426.872 Da.

1   GLYSERTHRASNALAGLUPROVALVALGLY
2   SERARGASPTHRMETPHETHRLYSILEPHE
3   VALGLYGLYLEUPROTYRHISTHRSERASP
4   LYSTHRLEUHISGLUTYRPHEGLUGLNPHE
5   GLYASPILEGLUGLUALAVALVALILETHR
6   ASPARGASNTHRGLNLYSSERARGGLYTYR
7   GLYPHEVALTHRMETLYSASPARGALASER
8   ALAGLUARGALACYSLYSASPPROASNPRO
9   ILEILEASPGLYARGLYSALAASNVALASN
10   LEUALATYRLEUGLYALALYSPROARGTHR
11   ASNVALGLN

Entity 2, RNA 6 residues - Formula weight is not available

1   GUGUGC

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.6 mM; RNA 0.72 mM; H2O 90%; D2O 10%; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%

sample_conditions_1: ionic strength: 0.1 M; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_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 NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

AMBER v9, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 18845 18846 19653
PDB
EMBL CCD71425 CCD71429
GB EFO82252 EGT29982 KIH66793
REF NP_001129938 NP_508674 XP_003117654

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