BMRB Entry 19249

Name: NMR structure of the PAI subdomain of Sleeping Beauty transposase
Published: 2013-12-16

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PDB ID: 2m8e
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19249
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR structure of the PAI subdomain of Sleeping Beauty transposase

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:

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).
PubMed: 24243759

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: ASMGKSKEISQDLRKKIVDL HKSGSSLGAISKRLKVPRSS VQTIVRKYKHHGTTQHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	54
1H chemical shifts	322

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PAI subdomain of Sleeping Beauty transposase	1

Entities:

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

1

ALA

SER

MET

GLY

LYS

SER

LYS

GLU

ILE

SER

2

GLN

ASP

LEU

ARG

LYS

ILE

VAL

ASP

LEU

3

HIS

LYS

SER

GLY

SER

LEU

GLY

ALA

ILE

4

SER

LYS

ARG

LEU

LYS

VAL

PRO

ARG

SER

5

VAL

GLN

THR

ILE

VAL

ARG

LYS

TYR

LYS

HIS

6

HIS

GLY

THR

GLN

HIS

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1

Software:

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

NMR spectrometers:

Bruker Avance 950 MHz

PDB	2M8E
EMBL	CDQ61086 CDQ84631
GB	AFR53956