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 11042

Title: Assigned chemical shifts of RelE

Deposition date: 2008-04-08 Original release date: 2010-03-11

Authors: Suzuki, Sakura; Kawazoe, Masahito; Kaminishi, Tatsuya; Takemoto, Chie; Muto, Yutaka; Shirouzu, Mikako; Yokoyama, Shigeyuki

Citation: Suzuki, Sakura; Kawazoe, Masahito; Kaminishi, Tatsuya; Takemoto, Chie; Muto, Yutaka; Shirouzu, Mikako; Yokoyama, Shigeyuki. "."  .

Assembly members:
RelE, polymer, 89 residues, 10745.523 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   Vector: pET11

Entity Sequences (FASTA):
RelE: MGYRIEFDPRAEKELEKLDR EVARRILRFLRERVATLEDP RSLGEPLRGPELGRFWKYRV GDYRLICHIQDREATVLVLR VGHARDVYR

Data sets:
Data typeCount
13C chemical shifts417
15N chemical shifts86
1H chemical shifts656

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RelE1

Entities:

Entity 1, RelE 89 residues - 10745.523 Da.

1   METGLYTYRARGILEGLUPHEASPPROARG
2   ALAGLULYSGLULEUGLULYSLEUASPARG
3   GLUVALALAARGARGILELEUARGPHELEU
4   ARGGLUARGVALALATHRLEUGLUASPPRO
5   ARGSERLEUGLYGLUPROLEUARGGLYPRO
6   GLULEUGLYARGPHETRPLYSTYRARGVAL
7   GLYASPTYRARGLEUILECYSHISILEGLN
8   ASPARGGLUALATHRVALLEUVALLEUARG
9   VALGLYHISALAARGASPVALTYRARG

Samples:

sample_1: RelE, [U-100% 13C; U-100% 15N], 0.4 mM; d-Tris-HCl, [U-2H], 20 mM; sodium chloride 100 mM; d-DTT, [U-2H], 5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

xwinnmr v3.5, Bruker Biospin - collection

NMRPipe v20060702, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView v5.0.4, Johnson, One Moon Scientific - data analysis

Kujira v0.9839, Kobayashi, N. - data analysis

Olivia v1.14.3, Yokochi, M - chemical shift assignment

CYANA v2.0.17, Guntert, Mumenthaler and Wuthrich - structure solution

SPARKY v3.110, Goddard - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAD12123 BAD72060
REF NP_990873 WP_011171672 WP_011279285 YP_001688116 YP_145503

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