BMRB Entry 16121

Title:
Structure of Archaeal L14e Ribosomal Protein from Sulfolobus sulfataricus
Deposition date:
2009-01-14
Original release date:
2009-05-20
Authors:
Edmondson, Stephen; Shriver, John
Citation:

Citation: Edmondson, Stephen; Turri, Jacquelyn; Smith, Kelley; Clark, Andrew; Shriver, John. "Structure, Stability, and Flexibility of Ribosomal Protein L14e from Sulfolobus solfataricus"  Biochemistry 48, 5553-5562 (2009).
PubMed: 19432457

Assembly members:

Assembly members:
L14e_ribosomal_protein, polymer, 96 residues, 10881.970 Da.

Natural source:

Natural source:   Common Name: Sulfolobus solfataricus   Taxonomy ID: 2287   Superkingdom: Archaea   Kingdom: not available   Genus/species: Sulfolobus solfataricus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETBlue-2

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts420
15N chemical shifts91
1H chemical shifts684

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1L14e_ribosomal_protein1

Entities:

Entity 1, L14e_ribosomal_protein 96 residues - 10881.970 Da.

1   METPROALAILEGLUVALGLYARGILECYS
2   VALLYSVALLYSGLYARGGLUALAGLYSER
3   LYSCYSVALILEVALASPILEILEASPASP
4   ASNPHEVALLEUVALTHRGLYPROLYSASP
5   ILETHRGLYVALLYSARGARGARGVALASN
6   ILELEUHISLEUGLUPROTHRASPLYSLYS
7   ILEASPILEGLNLYSGLYALASERASPGLU
8   GLUVALLYSLYSLYSLEUGLUGLUSERASN
9   LEUTHRGLUTYRMETLYSGLULYSILELYS
10   ILEARGMETPROTHRLEU

Samples:

sample_h2o: L14e ribosomal protein, [U-100% 13C; U-100% 15N], 1 mM; D2O 10%; H2O 90%

sample_d2o: L14e ribosomal protein, [U-100% 13C; U-100% 15N], 1 mM; D2O 100%

sample_n15: L14e ribosomal protein, [U-100% 15N], 1.0 mM; DSS 0.2 mM; D2O 10%; H2O 90%

sample_rdc: L14e ribosomal protein, [U-100% 15N], 1 mM; C12E5 5%; hexanol 1.0 r; D2O 10%; H2O 90%

sample_conditions_standard: ionic strength: 0 M; pH: 5.0; pressure: 1.0 atm; temperature: 303.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_n15isotropicsample_conditions_standard
3D HNCOsample_h2oisotropicsample_conditions_standard
3D HNCACBsample_h2oisotropicsample_conditions_standard
3D CBCA(CO)NHsample_h2oisotropicsample_conditions_standard
3D HNCAsample_h2oisotropicsample_conditions_standard
3D HN(CO)CAsample_h2oisotropicsample_conditions_standard
3D HNHAsample_h2oisotropicsample_conditions_standard
3D HCC_TOCSY-NNHsample_h2oisotropicsample_conditions_standard
3D CCC-TOCSY-NNHsample_h2oisotropicsample_conditions_standard
3D HCCH-TOCSYsample_d2oisotropicsample_conditions_standard
3D HCCH-COSYsample_d2oisotropicsample_conditions_standard
HBCBCGCDHDsample_h2oisotropicsample_conditions_standard
2D DQF-COSYsample_h2oisotropicsample_conditions_standard
2D 1H-1H NOESYsample_h2oisotropicsample_conditions_standard
2D 1H-13C HSQCsample_h2oisotropicsample_conditions_standard
3D 1H-15N NOESYsample_h2oisotropicsample_conditions_standard
3D 1H-13C NOESYsample_d2oisotropicsample_conditions_standard
2D 1H-15N HSQCsample_d2oisotropicsample_conditions_standard
2D 1H-15N NOEsample_h2oisotropicsample_conditions_standard
2D 1H-15N T1sample_h2oisotropicsample_conditions_standard
2D 1H-15N T1rhosample_h2oisotropicsample_conditions_standard
3D HNCO-IPAPsample_rdcanisotropicsample_conditions_standard

Software:

VNMR, Varian - collection

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

NMRView vaqua, Johnson, One Moon Scientific - chemical shift assignment, peak picking

ARIA v1.2, Linge, O'Donoghue and Nilges - chemical shift assignment

X-PLOR NIH v2.19, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 500 MHz

Related Database Links:

BMRB 15210
PDB
GB AAK40722 ACX91605 AKA73699 AKA76396 AKA79089
REF WP_009988801
SP Q980C1
AlphaFold Q980C1

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