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 19249

Title: NMR structure of the PAI subdomain of Sleeping Beauty transposase   PubMed: 24243759

Deposition date: 2013-05-17 Original release date: 2013-12-16

Authors: Eubanks, Claire; Schreifels, Jeff; Aronovich, Elena; Carlson, Daniel; Hacjkett, Perry; Nesmelova, Irina

Citation: Carpentier, Claire; Schreifels, Jeffrey; Aronovich, Elena; Carlson, Daniel; Hackett, Perry; Nesmelova, Irina. "NMR structural analysis of Sleeping Beauty transposase binding to DNA."  Protein Sci. 23, 23-33 (2014).

Assembly members:
entity, polymer, 57 residues, 6394.522 Da.

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

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

Entity Sequences (FASTA):
entity: ASMGKSKEISQDLRKKIVDL HKSGSSLGAISKRLKVPRSS VQTIVRKYKHHGTTQHH

Data sets:
Data typeCount
15N chemical shifts54
1H chemical shifts322

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PAI subdomain of Sleeping Beauty transposase1

Entities:

Entity 1, PAI subdomain of Sleeping Beauty transposase 57 residues - 6394.522 Da.

1   ALASERMETGLYLYSSERLYSGLUILESER
2   GLNASPLEUARGLYSLYSILEVALASPLEU
3   HISLYSSERGLYSERSERLEUGLYALAILE
4   SERLYSARGLEULYSVALPROARGSERSER
5   VALGLNTHRILEVALARGLYSTYRLYSHIS
6   HISGLYTHRTHRGLNHISHIS

Samples:

sample_1: entity, [U-100% 15N], 0.15 mM; sodium phosphate 20 mM; H2O 90%; D2O 10%

sample_2: entity, [U-100% 15N], 0.15 mM; sodium phosphate 20 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 20 mM; pH: 7; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

  • Bruker Avance 950 MHz

Related Database Links:

PDB
EMBL CDQ61086 CDQ84631
GB AFR53956

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