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 4688

Title: Assignment and secondary structure identification of the ribosomal protein L18 from Thermus thermophilus

Deposition date: 2000-03-15 Original release date: 2000-07-07

Authors: Woestenenk, Esmeralda; Allard, Peter; Gongadze, George; Moskalenko, Svetlana; Shcherbakov, Dmitry; Rak, Alexey; Garber, Maria; Hard, Torleif; Berglund, Helena

Citation: Woestenenk, Esmeralda; Allard, Peter; Gongadze, George; Moskalenko, Svetlana; Shcherbakov, Dmitry; Rak, Alexey; Garber, Maria; Hard, Torleif; Berglund, Helena. "Letter to the Editor: Assignment and secondary structure identification of the ribosomal protein L18 from Thermus thermophilus"  J. Biomol. NMR 17, 273-274 (2000).

Assembly members:
L18, polymer, 111 residues, 12480 Da.

Natural source:   Common Name: Thermus thermophilus   Taxonomy ID: 274   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Thermus thermophilus

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

Entity Sequences (FASTA):
L18: ARLTAYERRKFRVRNRIKRT GRLRLSVFRSLKHIYAQIID DEKGVTLVSASSLALKLKGN KTEVARQVGRALAEKALALG IKQVAFDRGPYKYHGRVKAL AEGAREGGLEF

Data sets:
Data typeCount
1H chemical shifts704
13C chemical shifts343
15N chemical shifts111

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1L181

Entities:

Entity 1, L18 111 residues - 12480 Da.

1   ALAARGLEUTHRALATYRGLUARGARGLYS
2   PHEARGVALARGASNARGILELYSARGTHR
3   GLYARGLEUARGLEUSERVALPHEARGSER
4   LEULYSHISILETYRALAGLNILEILEASP
5   ASPGLULYSGLYVALTHRLEUVALSERALA
6   SERSERLEUALALEULYSLEULYSGLYASN
7   LYSTHRGLUVALALAARGGLNVALGLYARG
8   ALALEUALAGLULYSALALEUALALEUGLY
9   ILELYSGLNVALALAPHEASPARGGLYPRO
10   TYRLYSTYRHISGLYARGVALLYSALALEU
11   ALAGLUGLYALAARGGLUGLYGLYLEUGLU
12   PHE

Samples:

sample_1: L18, [U-13C; U-15N], 0.7 – 1.6 mM

conditions_1: pH: 5.9; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
HNCAsample_1not availableconditions_1
HN(CO)CAsample_1not availableconditions_1
HNCACBsample_1not availableconditions_1
CBCA(CO)NHsample_1not availableconditions_1
(H)C(CO)NHsample_1not availableconditions_1
H(CCO)NHsample_1not availableconditions_1
HCCH-TOCSYsample_1not availableconditions_1
HCCH-COSYsample_1not availableconditions_1
1H-15N-TOCSYsample_1not availableconditions_1
1H-15N-NOESYsample_1not availableconditions_1
2D NOESYsample_1not availableconditions_1

Software:

No software information available

NMR spectrometers:

  • Varian Inova 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAD71499
EMBL CAA62289
GB AAS81654 AEG34089 AFH38278 EIA38537
REF WP_008633391 YP_144942
SP P80320 Q5SHQ4 Q72I20

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