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 19098

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19098
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: Sidechain and backbone NMR resonance assignment for the RNA binding and C-terminal domain of the ribosome assembly factor Nop6 from S. cerevisiae

Deposition date: 2013-03-18 Original release date: 2016-04-12

Authors: Wurm, Jan; Lioutikov, Anatoli; Koetter, Peter; Entian, Karl-Dieter; Woehnert, Jens

Citation: Wurm, Jan; Lioutikov, Anatoli; Koetter, Peter; Entian, Karl-Dieter; Woehnert, Jens. "Backbone and sidechain NMR assignments for the ribosome assembly factor Nop6 from Saccharomyces cerevisiae"  Biomol. NMR Assignments ., .-..

Assembly members:
Nop6, polymer, 132 residues, Formula weight is not available

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

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

Entity Sequences (FASTA):
Nop6: gnrfivfvgslprditavel qnhfknsspdqirlradkgi aflefdadkdrtgiqrrmdi allqhgtllkekkinveltv ggggnsqerleklknknikl deerkerltkmindgnqkki akttataaqtsg

Data sets:
Data typeCount
13C chemical shifts581
15N chemical shifts136
1H chemical shifts936

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Nop61

Entities:

Entity 1, Nop6 132 residues - Formula weight is not available

residues 75-206 of Saccharomyces cerevisiae Nop6

1   GLYASNARGPHEILEVALPHEVALGLYSER
2   LEUPROARGASPILETHRALAVALGLULEU
3   GLNASNHISPHELYSASNSERSERPROASP
4   GLNILEARGLEUARGALAASPLYSGLYILE
5   ALAPHELEUGLUPHEASPALAASPLYSASP
6   ARGTHRGLYILEGLNARGARGMETASPILE
7   ALALEULEUGLNHISGLYTHRLEULEULYS
8   GLULYSLYSILEASNVALGLULEUTHRVAL
9   GLYGLYGLYGLYASNSERGLNGLUARGLEU
10   GLULYSLEULYSASNLYSASNILELYSLEU
11   ASPGLUGLUARGLYSGLUARGLEUTHRLYS
12   METILEASNASPGLYASNGLNLYSLYSILE
13   ALALYSTHRTHRALATHRALAALAGLNTHR
14   SERGLY

Samples:

sample_1: H2O 90%; D2O 10%; Nop6, U-15N, 0.8 mM; KH2PO4 2 mM; Na2HPO4 8 mM; NaCl 100 mM; KCl 2.7 mM

sample_2: H2O 90%; D2O 10%; Nop6, U-15N/U-13C, 0.8 mM; KH2PO4 2 mM; Na2HPO4 8 mM; NaCl 100 mM; KCl 2.7 mM

sample_conditions_1: ionic strength: 130 mM; pH: 6.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCACOsample_2isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1

Software:

TOPSPIN v2.1 - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz

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