BMRB Entry 19554

Title:
Domain 2 of E. coli ribosomal protein S1
Deposition date:
2013-10-12
Original release date:
2014-04-14
Authors:
GIRAUD, Pierre; CRECHET, Jean-Bernard; BONTEMS, Francois; UZAN, Marc; SIZUN, Christina
Citation:

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).
PubMed: 24682851

Assembly members:

Assembly members:
S1F12, polymer, 182 residues, 10462.053 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15b

Data sets:
Data typeCount
13C chemical shifts668
15N chemical shifts174
1H chemical shifts1088

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1S1F121

Entities:

Entity 1, S1F12 182 residues - 10462.053 Da.

This sequence contains the two first domains of S1 separated by a flexible linker and an extended flexible N-terminal region

1   GLYSERHISMETTHRGLUSERPHEALAGLN
2   LEUPHEGLUGLUSERLEULYSGLUILEGLU
3   THRARGPROGLYSERILEVALARGGLYVAL
4   VALVALALAILEASPLYSASPVALVALLEU
5   VALASPALAGLYLEULYSSERGLUSERALA
6   ILEPROALAGLUGLNPHELYSASNALAGLN
7   GLYGLULEUGLUILEGLNVALGLYASPGLU
8   VALASPVALALALEUASPALAVALGLUASP
9   GLYPHEGLYGLUTHRLEULEUSERARGGLU
10   LYSALALYSARGHISGLUALATRPILETHR
11   LEUGLULYSALATYRGLUASPALAGLUTHR
12   VALTHRGLYVALILEASNGLYLYSVALLYS
13   GLYGLYPHETHRVALGLULEUASNGLYILE
14   ARGALAPHELEUPROGLYSERLEUVALASP
15   VALARGPROVALARGASPTHRLEUHISLEU
16   GLUGLYLYSGLULEUGLUPHELYSVALILE
17   LYSLEUASPGLNLYSARGASNASNVALVAL
18   VALSERARGARGALAVALILEGLUSERGLU
19   ASNSER

Samples:

S1F12-15N13C2H: S1F12, [U-99% 13C; U-99% 15N; U-80% 2H], 0.25 ± 0.025 mM; sodium phosphate 25.0 ± 1.0 mM; sodium chloride 200.0 ± 2.0 mM; H2O 93%; D2O, [U-100% 2H], 7%

S1F12-15N13C-H2O: S1F12, [U-99% 13C; U-99% 15N], 0.2 ± 0.02 mM; potassium phosphate 50.0 ± 1.0 mM; potassium chloride 200.0 ± 2.0 mM; H2O 93%; D2O, [U-100% 2H], 7%

S1F12-15N13C-D2O: S1F12, [U-99% 13C; U-99% 15N], 0.2 ± 0.02 mM; potassium phosphate 50.0 ± 1.0 mM; potassium chloride 200.0 ± 2.0 mM; D2O, [U-100% 2H], 100%

Condition_1: ionic strength: 0.200 M; pH: 6.800; pressure: 1.000 atm; temperature: 293.000 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCS1F12-15N13C2HisotropicCondition_1
3D HNCAS1F12-15N13C2HisotropicCondition_1
3D HN(CO)CAS1F12-15N13C2HisotropicCondition_1
3D HNCACBS1F12-15N13C2HisotropicCondition_1
3D CBCA(CO)NHS1F12-15N13C2HisotropicCondition_1
3D HNCOS1F12-15N13C2HisotropicCondition_1
3D HN(CA)COS1F12-15N13C2HisotropicCondition_1
2D 1H-15N HSQCS1F12-15N13C-H2OisotropicCondition_1
3D HBHA(CO)NHS1F12-15N13C-H2OisotropicCondition_1
3D 1H-15N NOESYS1F12-15N13C-H2OisotropicCondition_1
2D 1H-13C HSQCS1F12-15N13C-D2OisotropicCondition_1
3D HCCH-TOCSYS1F12-15N13C-D2OisotropicCondition_1
3D HCCH-TOCSY aromaticS1F12-15N13C-D2OisotropicCondition_1
3D CCH-TOCSYS1F12-15N13C-D2OisotropicCondition_1
2D 1H-1H TOCSYS1F12-15N13C-D2OisotropicCondition_1
2D 1H-1H NOESYS1F12-15N13C-D2OisotropicCondition_1
3D 1H-13C NOESYS1F12-15N13C-D2OisotropicCondition_1

Software:

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

TOPSPIN v3.1, Bruker, Herrmann, G?ntert and W?thrich - 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:

UNP P0AG67
BMRB 19550
PDB
DBJ BAA35655 BAB34417 BAG76494 BAH62634 BAI24353
EMBL CAA23630 CAA23644 CAD05381 CAO97188 CAP75381
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 P77352 P0AG69 P0AG67 P0AG68 P0AG70

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