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 19550

Title: Domain 1 of E. coli ribosomal protein S1   PubMed: 24682851

Deposition date: 2013-10-11 Original release date: 2014-04-14

Authors: GIRAUD, Pierre; CRECHET, Jean-Bernard; BONTEMS, Francois; UZAN, Marc; SIZUN, Christina

Citation: Giraud, Pierre; Crechet, Jean-Bernard; Uzan, Marc; Bontems, Francois; Sizun, Christina. "Resonance assignment of the ribosome binding domain of E. coli ribosomal protein S1."  Biomol. NMR Assignments ., .-. (2014).

Assembly members:
S1F1, polymer, 96 residues, 10408.6085 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET151:D-TOPO

Entity Sequences (FASTA):
S1F1: GIDPFTESLKEIETRPGSIV RGVVVAIDKDVVLVDAGLKS ESAIPAEQFKNAQGELEIQV GDEVDVALDAVEDGFGETLL SREKAKRHEAWITLEK

Data sets:
Data typeCount
13C chemical shifts389
15N chemical shifts95
1H chemical shifts659

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1S1F11

Entities:

Entity 1, S1F1 96 residues - 10408.6085 Da.

The six first residues are generated by TOPO cloning and TEV cleavage.

1   GLYILEASPPROPHETHRGLUSERLEULYS
2   GLUILEGLUTHRARGPROGLYSERILEVAL
3   ARGGLYVALVALVALALAILEASPLYSASP
4   VALVALLEUVALASPALAGLYLEULYSSER
5   GLUSERALAILEPROALAGLUGLNPHELYS
6   ASNALAGLNGLYGLULEUGLUILEGLNVAL
7   GLYASPGLUVALASPVALALALEUASPALA
8   VALGLUASPGLYPHEGLYGLUTHRLEULEU
9   SERARGGLULYSALALYSARGHISGLUALA
10   TRPILETHRLEUGLULYS

Samples:

S1F1-15N13C-H2O: S1F1, [U-99% 13C; U-99% 15N], 0.2 ± 2e-05 mM; potassium phosphate 25.0 ± 0.0025 mM; potassium chloride 200.0 ± 0.0025 mM; H2O 93%; D2O, [U-100% 2H], 7%

S1F1-15N13C-D2O: S1F1, [U-99% 13C; U-99% 15N], 0.2 ± 2e-05 mM; potassium phosphate 25.0 ± 0.0025 mM; potassium chloride 200.0 ± 0.0025 mM; D2O, [U-100% 2H], 100%

S1F1-15N: S1F1, [U-99% 13C; U-99% 15N], 0.5 ± 2e-05 mM; potassium phosphate 25.0 ± 0.0025 mM; potassium chloride 200.0 ± 0.0025 mM; H2O 93%; D2O, [U-100% 2H], 7%

Condition_1: ionic strength: 0.200 M; pH: 6.500; pressure: 1.000 atm; temperature: 293.000 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCS1F1-15N13C-H2OisotropicCondition_1
3D HNCAS1F1-15N13C-H2OisotropicCondition_1
3D HN(CO)CAS1F1-15N13C-H2OisotropicCondition_1
3D HNCACBS1F1-15N13C-H2OisotropicCondition_1
3D HCCH-TOCSYS1F1-15N13C-D2OisotropicCondition_1
3D HNCOS1F1-15N13C-H2OisotropicCondition_1
3D HN(CA)COS1F1-15N13C-H2OisotropicCondition_1
3D 1H-15N NOESYS1F1-15NisotropicCondition_1
3D 1H-13C NOESYS1F1-15N13C-D2OisotropicCondition_1
2D 1H-13C HSQCS1F1-15N13C-D2OisotropicCondition_1
3D CCH-TOCSYS1F1-15N13C-D2OisotropicCondition_1
3D HCCH-TOCSY aromaticS1F1-15N13C-D2OisotropicCondition_1
2D 1H-1H NOESYS1F1-15N13C-D2OisotropicCondition_1

Software:

CCPNmr ANALYSIS v2.2, CCPN - Spectrum analysis, Spectrum display

TOPSPIN v3.1, Bruker, Guntert, Mumenthaler and Wuthrich - Spectrum processing, Structure calculation

NMRPipe vany, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - Spectrum processing

TALOS+ vany, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - Dihedral angles

NMR spectrometers:

  • Bruker Avance 950 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

UniProt P0AG67
BMRB 19554
PDB
DBJ BAA35655 BAB34417 BAG76494 BAH62634 BAI24353
EMBL CAA23630 CAA23644 CAD05381 CAP75381 CAQ31439
GB AAC73997 AAG55396 AAL19915 AAN42537 AAN79519
PIR AC0614
PRF 0804233A
REF NP_309021 NP_415431 NP_455468 NP_459956 NP_706830
SP P0AG67 P0AG68 P0AG69 P0AG70
AlphaFold P0AG67

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