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 17675

Title: Backbone 1H,15N,13C and 13CB chemical shifts of folded state and denatured state for the N-terminal domain of ribosomal protein L9 (NTL9) V3AI4A double mutant   PubMed: 21915914

Authors: Meng, Wenli; Raleigh, Daniel

Citation: Meng, Wenli; Raleigh, Daniel. "Analysis of electrostatic interactions in the denatured state ensemble of the N-terminal domain of L9 under native conditions."  Proteins 79, 3500-3510 (2011).

Assembly members:
NTL9_V3AI4A, polymer, 56 residues, Formula weight is not available

Natural source:   Common Name: Geobacillus stearothermophilus   Taxonomy ID: 1422   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Geobacillus stearothermophilus

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

Entity Sequences (FASTA):
NTL9_V3AI4A: MKAAFLKDVKGKGKKGEIKN VADGYANNFLFKQGLAIEAT PANLKALEAQKQKEQR

Data sets:
Data typeCount
13C chemical shifts317
15N chemical shifts105
1H chemical shifts210

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1folded state1
2denatured state1

Entities:

Entity 1, folded state 56 residues - Formula weight is not available

1   METLYSALAALAPHELEULYSASPVALLYS
2   GLYLYSGLYLYSLYSGLYGLUILELYSASN
3   VALALAASPGLYTYRALAASNASNPHELEU
4   PHELYSGLNGLYLEUALAILEGLUALATHR
5   PROALAASNLEULYSALALEUGLUALAGLN
6   LYSGLNLYSGLUGLNARG

Samples:

15N_sample: NTL9_V3AI4A, [U-99% 15N], 0.5 mM; DSS 0.4 mM; sodium chloride 100 mM; sodium acetate, [U-99% 2H], 20 mM; H2O 90%; D2O 10%

13C15N_sample: NTL9_V3AI4A, [U-99% 13C; U-99% 15N], 0.5 mM; DSS 0.4 mM; sodium chloride 100 mM; sodium acetate, [U-99% 2H], 20 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.12 M; pH: 5.5; pressure: 1 atm; temperature: 285 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15N_sampleisotropicsample_conditions_1
2D 1H-15N HSQC15N_sampleisotropicsample_conditions_1
3D CBCA(CO)NH13C15N_sampleisotropicsample_conditions_1
3D CBCA(CO)NH13C15N_sampleisotropicsample_conditions_1
3D HNCACB13C15N_sampleisotropicsample_conditions_1
3D HNCACB13C15N_sampleisotropicsample_conditions_1
3D HNCO13C15N_sampleisotropicsample_conditions_1
3D 1H-15N TOCSY15N_sampleisotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 18918