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 30680

Title: Sleeping Beauty transposase PAI subdomain mutant - H19Y

Deposition date: 2019-10-24 Original release date: 2020-10-23

Authors: Nesmelova, I.; Leighton, G.; Yan, C.; Lustig, J.; Corona, R.; Guo, J.; Ivics, Z.

Citation: Nesmelova, I.; Leighton, G.; Yan, C.; Lustig, J.; Corona, R.; Guo, J.; Ivics, Z.. "H19Y mutation in the primary DNA-recognition subdomain of the Sleeping Beauty transposase improves structural stability, transposon DNA-binding and transposition"  . ., .-..

Assembly members:
entity_1, polymer, 57 residues, 6389.402 Da.

Natural source:   Common Name: Rainbow trout   Taxonomy ID: 8022   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Oncorhynchus mykiss

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

Entity Sequences (FASTA):
entity_1: ASMGKSKEISQDLRKRIVDL YKSGSSLGAISKRLAVPRSS VQTIVRKYKHHGTTQHH

Data sets:
Data typeCount
13C chemical shifts143
15N chemical shifts55
1H chemical shifts360

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 57 residues - 6389.402 Da.

1   ALASERMETGLYLYSSERLYSGLUILESER
2   GLNASPLEUARGLYSARGILEVALASPLEU
3   TYRLYSSERGLYSERSERLEUGLYALAILE
4   SERLYSARGLEUALAVALPROARGSERSER
5   VALGLNTHRILEVALARGLYSTYRLYSHIS
6   HISGLYTHRTHRGLNHISHIS

Samples:

sample_1: pai subdomain mutant, [U-13C; U-15N], 0.5 mM

sample_conditions_1: ionic strength: 25 mM; pH: 5; pressure: 1 atm; temperature: 278 K

sample_conditions_2: ionic strength: 25 mM; pH: 5; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_2
3D CBCA(CO)NHsample_1isotropicsample_conditions_2
3D HNCACBsample_1isotropicsample_conditions_2

Software:

CARA, Keller and Wuthrich - chemical shift assignment

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

NMRView, Johnson, One Moon Scientific - data analysis

NMR spectrometers:

  • Bruker AVANCE III 700 MHz
  • Bruker AVANCE III 950 MHz

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