BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 15210

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15210
MolProbity Validation Chart

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Title: NMR Structure of 50S Ribosomal Protein L14e from Sulfolobus Solfataricus; Northeast Structural Genomics Consortium Target SSR105.

Deposition date: 2007-04-10 Original release date: 2007-06-05

Authors: Singarapu, Kiran Kumar; Wu, Yibing; Yee, Adelinda; semesi, Anthony; Arrowsmith, cheryl; Szyperski, Thomas

Citation: Singarapu, Kiran Kumar; Wu, Yibing; Yee, Adelinda; semesi, Anthony; Arrowsmith, cheryl; Szyperski, Thomas. "NMR Structure of 50S Ribosomal Protein L14e from Sulfolobus Solfataricus; Northeast Structural Genomics Consortium Target SSR105."  The BMRB entry is the only known published source for the data..

Assembly members:
50s ribosomal protein l14e, polymer, 96 residues, 10886.001 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: E. coli - cell free

Entity Sequences (FASTA):
50s ribosomal protein l14e: MPAIEVGRICVKVKGREAGS KCVIVDIIDDNFVLVTGPKD ITGVKRRRVNILHLEPTDKK IDIQKGASDEEVKKKLEESN LTEYMKEKIKIRMPTL

Data sets:
Data typeCount
13C chemical shifts432
15N chemical shifts95
1H chemical shifts722

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
150s ribosomal protein l14e1

Entities:

Entity 1, 50s ribosomal protein l14e 96 residues - 10886.001 Da.

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

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.5 mM; H2O 90%; D2O 10%

sample_2: entity, [U-10% 13C; U-99% 15N], 0.5 mM

sample_conditions_1: ionic strength: 320 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
4,3 D GFT HCCH COFYsample_1isotropicsample_conditions_1
3D HCCH COSYsample_1isotropicsample_conditions_1
3D Simultanious NOESYsample_1isotropicsample_conditions_1

Software:

VNMR, Varian - collection

AutoAssign, Zimmerman, Moseley, Kulikowski, Montelione - chemical shift assignment

AutoStruct, Huang, Swapana, Rajan, Ke, Xia, Shukla, Inouye and Montelione - chemical shift assignment

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - refinement

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

Molmol, Koradi, Billeter and Wuthrich - structure display

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian Avance 600 MHz

Related Database Links:

BMRB 16121
PDB
GB AAK40722 ACX91605 AKA73699 AKA76396 AKA79089
REF WP_009988801
SP Q980C1

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