BMRB Entry 30680

Name: Sleeping Beauty transposase PAI subdomain mutant - H19Y
Published: 2020-10-23

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30680

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	143
15N chemical shifts	55
1H chemical shifts	360

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 57 residues - 6389.402 Da.

1

ALA

SER

MET

GLY

LYS

SER

LYS

GLU

ILE

SER

2

GLN

ASP

LEU

ARG

LYS

ARG

ILE

VAL

ASP

LEU

3

TYR

LYS

SER

GLY

SER

LEU

GLY

ALA

ILE

4

SER

LYS

ARG

LEU

ALA

VAL

PRO

ARG

SER

5

VAL

GLN

THR

ILE

VAL

ARG

LYS

TYR

LYS

HIS

6

HIS

GLY

THR

GLN

HIS

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:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_2
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_2
3D HNCACB	sample_1	isotropic	sample_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