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 10095

Title: Solution structure of the KH domain of human ribosomal protein S3

Deposition date: 2007-02-13 Original release date: 2008-08-29

Authors: Nameki, N.; Tomizawa, T.; Koshiba, S.; Kigawa, T.; Yokoyama, S.

Citation: Nameki, N.; Tomizawa, T.; Koshiba, S.; Kigawa, T.; Yokoyama, S.. "Solution structure of the KH domain of human ribosomal protein S3"  .

Assembly members:
40S ribosomal protein S3, polymer, 92 residues, Formula weight is not available

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

Experimental source:   Production method: cell free synthesis   Vector: P040301-10

Entity Sequences (FASTA):
40S ribosomal protein S3: GSSGSSGFKAELNEFLTREL AEDGYSGVEVRVTPTRTEII ILATRTQNVLGEKGRRIREL TAVVQKRFGFPEGSVELYAE KVATRGSGPSSG

Data sets:
Data typeCount
13C chemical shifts362
15N chemical shifts81
1H chemical shifts572

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
140S ribosomal protein S31

Entities:

Entity 1, 40S ribosomal protein S3 92 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYPHELYSALA
2   GLULEUASNGLUPHELEUTHRARGGLULEU
3   ALAGLUASPGLYTYRSERGLYVALGLUVAL
4   ARGVALTHRPROTHRARGTHRGLUILEILE
5   ILELEUALATHRARGTHRGLNASNVALLEU
6   GLYGLULYSGLYARGARGILEARGGLULEU
7   THRALAVALVALGLNLYSARGPHEGLYPHE
8   PROGLUGLYSERVALGLULEUTYRALAGLU
9   LYSVALALATHRARGGLYSERGLYPROSER
10   SERGLY

Samples:

sample_1: KH domain, [U-13C; U-15N], 0.6 mM; d-Tris-HCl 20 mM; NaCl 200 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 220 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYsample_1isotropiccondition_1
3D 13C-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20020425, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.901, Kobayashi, N. - data analysis

CYANA v1.0.7, Guntert, P. - structure solution

OPALp, Billeter, M., Guntert, P., Koradi, R. - refinement

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAB22624 BAB27042 BAB27761 BAB28111 BAB28159
EMBL CAA35916 CAA39248 CAA40592 CAA54167 CAA84290
GB AAA18095 AAB19349 AAB46849 AAB60336 AAB60337
REF NP_000996 NP_001009239 NP_001026007 NP_001029219 NP_001038066
SP E2RH47 P02350 P23396 P47835 P62908
TPG DAA21909
AlphaFold E2RH47 P02350 P23396 P47835 P62908

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