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 10140

Title: Backbone NMR assignments of of RimM complexed with rS19   PubMed: 17616598

Deposition date: 2007-06-13 Original release date: 2008-06-12

Authors: Suzuki, S.; Tatsuguchi, A.; Matsumoto, E.; Kawazoe, M.; Kaminishi, T.; Shirouzu, M.; Muto, Y.; Takemoto, C.; Yokoyama, S.

Citation: Suzuki, S.; Tatsuguchi, A.; Matsumoto, E.; Kawazoe, M.; Kaminishi, T.; Shirouzu, M.; Muto, Y.; Takemoto, C.; Yokoyama, S.. "Structural characterization of the ribosome maturation protein, RimM"  J. Bacteriol. 189, .-6397 (6406).

Assembly members:
RimM, polymer, 162 residues, Formula weight is not available
rS19, polymer, 93 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
RimM: MRLVEIGRFGAPYALKGGLR FRGEPVVLHLERVYVEGHGW RAIEDLYRVGEELVVHLAGV TDRTLAEALVGLRVYAEVAD LPPLEEGRYYYFALIGLPVY VEGRQVGEVVDILDAGAQDV LIIRGVGERLRDRAERLVPL QAPYVRVEEGSIHVDPIPGL FD
rS19: MPRSLKKGVFVDDHLLEKVL ELNAKGEKRLIKTWSRRSTI VPEMVGHTIAVYNGKQHVPV YITENMVGHKLGEFAPTRTY RGHGKEAKATKKK

Data sets:
Data typeCount
13C chemical shifts156
15N chemical shifts141
1H chemical shifts141

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RimM1
2rS192

Entities:

Entity 1, RimM 162 residues - Formula weight is not available

1   METARGLEUVALGLUILEGLYARGPHEGLY
2   ALAPROTYRALALEULYSGLYGLYLEUARG
3   PHEARGGLYGLUPROVALVALLEUHISLEU
4   GLUARGVALTYRVALGLUGLYHISGLYTRP
5   ARGALAILEGLUASPLEUTYRARGVALGLY
6   GLUGLULEUVALVALHISLEUALAGLYVAL
7   THRASPARGTHRLEUALAGLUALALEUVAL
8   GLYLEUARGVALTYRALAGLUVALALAASP
9   LEUPROPROLEUGLUGLUGLYARGTYRTYR
10   TYRPHEALALEUILEGLYLEUPROVALTYR
11   VALGLUGLYARGGLNVALGLYGLUVALVAL
12   ASPILELEUASPALAGLYALAGLNASPVAL
13   LEUILEILEARGGLYVALGLYGLUARGLEU
14   ARGASPARGALAGLUARGLEUVALPROLEU
15   GLNALAPROTYRVALARGVALGLUGLUGLY
16   SERILEHISVALASPPROILEPROGLYLEU
17   PHEASP

Entity 2, rS19 93 residues - Formula weight is not available

1   METPROARGSERLEULYSLYSGLYVALPHE
2   VALASPASPHISLEULEUGLULYSVALLEU
3   GLULEUASNALALYSGLYGLULYSARGLEU
4   ILELYSTHRTRPSERARGARGSERTHRILE
5   VALPROGLUMETVALGLYHISTHRILEALA
6   VALTYRASNGLYLYSGLNHISVALPROVAL
7   TYRILETHRGLUASNMETVALGLYHISLYS
8   LEUGLYGLUPHEALAPROTHRARGTHRTYR
9   ARGGLYHISGLYLYSGLUALALYSALATHR
10   LYSLYSLYS

Samples:

sample_1: RimM, [U-13C; U-15N], 0.03 ± 0.001 mM; rS19 0.03 ± 0.001 mM; HEPES 20 ± 0.1 mM; D2O 10 ± 0.1 %; H2O 90 ± 0.1 %; NaCl 300 ± 1.0 mM

condition_1: ionic strength: 320 mM; pH: 7.0; pressure: 1 atm; temperature: 318 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYsample_1not availablecondition_1
3D HNCAsample_1not availablecondition_1
3D HN(CO)CAsample_1not availablecondition_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

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

Kujira v0.9321, Kobayashi, N. - data analysis

Olivia v1.10.5, Yokochi, M. - data analysis

SPARKY v3.110, Goddard, T.D., Kneller, D.G. - data analysis

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

BMRB 10138 10139
PDB
DBJ BAD70856
GB AAS81019 AEG33454 AFH38925 EIA39096
REF WP_008632437 WP_011228392 YP_144299
SP Q5SJH5 Q72JU7

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