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 17595

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/BMR17595
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: NMR resonance assignments for an archaeal homolog of the endonuclease Nob1 involved in ribosome biogenesis   PubMed: 22156373

Deposition date: 2011-04-19 Original release date: 2011-12-14

Authors: Veith, Thomas; Wurm, Jan; Duchardt-Ferner, Elke; Weis, Benjamin; Hennig, Raoul; Martin, Roman; Safferthal, Charlotta; Bohnsack, Markus; Schleiff, Enrico; Woehnert, Jens

Citation: Veith, Thomas; Martin, Roman; Wurm, Jan; Weis, Benjamin; Duchardt-Ferner, Elke; Safferthal, Charlotta; Hennig, Raoul; Mirus, Oliver; Bohnsack, Markus; Wohnert, Jens; Schleiff, Enrico. "Structural and functional analysis of the archaeal endonuclease Nob1."  Nucleic Acids Res. 40, 3259-3274 (2012).

Assembly members:
PhNob1, polymer, 161 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.

Natural source:   Common Name: Euryarchaeotes   Taxonomy ID: 53953   Superkingdom: Archaea   Kingdom: not available   Genus/species: Pyrococcus horikoshii

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

Entity Sequences (FASTA):
PhNob1: MLRNLKKTLVLDSSVFIQGI DIEGYTTPSVVEEIKDRESK IFLESLISAGKVKIAEPSKE SIDRIIQVAKETGEVNELSK ADIEVLALAYELKGEIFSDD YNVQNIASLLGLRFRTLKRG IKKVIKWRYVCIGCGRKFST LPPGGVCPDCGSKVKLIPRK R

Data sets:
Data typeCount
13C chemical shifts704
15N chemical shifts160
1H chemical shifts1097

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PhNob11
2Zn2

Entities:

Entity 1, PhNob1 161 residues - Formula weight is not available

1   METLEUARGASNLEULYSLYSTHRLEUVAL
2   LEUASPSERSERVALPHEILEGLNGLYILE
3   ASPILEGLUGLYTYRTHRTHRPROSERVAL
4   VALGLUGLUILELYSASPARGGLUSERLYS
5   ILEPHELEUGLUSERLEUILESERALAGLY
6   LYSVALLYSILEALAGLUPROSERLYSGLU
7   SERILEASPARGILEILEGLNVALALALYS
8   GLUTHRGLYGLUVALASNGLULEUSERLYS
9   ALAASPILEGLUVALLEUALALEUALATYR
10   GLULEULYSGLYGLUILEPHESERASPASP
11   TYRASNVALGLNASNILEALASERLEULEU
12   GLYLEUARGPHEARGTHRLEULYSARGGLY
13   ILELYSLYSVALILELYSTRPARGTYRVAL
14   CYSILEGLYCYSGLYARGLYSPHESERTHR
15   LEUPROPROGLYGLYVALCYSPROASPCYS
16   GLYSERLYSVALLYSLEUILEPROARGLYS
17   ARG

Entity 2, Zn - Zn - 65.409 Da.

1   ZN

Samples:

15N: PhNob1, [U-15N], 0.4 mM; potassium chloride 50 mM; BisTris 50 mM; H2O 90%; D2O 10%

sample_1: PhNob1, [U-13C; U-15N], 0.4 mM; potassium chloride 50 mM; BisTris 50 mM; H2O 90%; D20 10%

sample_conditions_1: ionic strength: 83 mM; pH: 6.2; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNHA15Nisotropicsample_conditions_1
3D 1H-15N NOESY15Nisotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - processing

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, structure solution

CARA v1.8.4.2, Keller and Wuthrich - chemical shift assignment

TALOS+, Cornilescu, Delaglio and Bax - structure solution

ATNOS, Herrmann, Guntert and Wuthrich - peak picking

CANDID, Herrmann, Guntert and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz
  • Bruker Avance 950 MHz

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