BMRB Entry 30239

Name: NMR structure of the RED subdomain of the Sleeping Beauty transposase
Published: 2017-06-02

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PDB ID: 5unk
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30239
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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:

NMR structure of the RED subdomain of the Sleeping Beauty transposase

Deposition date:

2017-01-31

Original release date:

2017-06-02

Authors:

Konnova, T.; Singer, C.; Nesmelova, I.

Citation:

Citation: Konnova, T.; Singer, C.; Nesmelova, I.. "NMR solution structure of the RED subdomain of the Sleeping Beauty transposase." Protein Sci. 26, 1171-1181 (2017).
PubMed: 28345263

Assembly members:

Assembly members:
entity_1, polymer, 62 residues, 7122.414 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: ASMVLSPRDERTLVRKVQIN PRTTAKDLVKMLEETGTKVS ISTVKRVLYRHNLKGRSARK LE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	164
15N chemical shifts	62
1H chemical shifts	404

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 62 residues - 7122.414 Da.

1

ALA

SER

MET

VAL

LEU

SER

PRO

ARG

ASP

GLU

2

ARG

THR

LEU

VAL

ARG

LYS

VAL

GLN

ILE

ASN

3

PRO

ARG

THR

ALA

LYS

ASP

LEU

VAL

LYS

4

MET

LEU

GLU

THR

GLY

THR

LYS

VAL

SER

5

ILE

SER

THR

VAL

LYS

ARG

VAL

LEU

TYR

ARG

6

HIS

ASN

LEU

LYS

GLY

ARG

SER

ALA

ARG

LYS

7

LEU

GLU

Samples:

sample_1: MES 20 mM; RED subdomain of the Sleeping Beauty transposase, [U-13C; U-15N], 2 mg/mL; sodium sulfate 650 mM

sample_2: MES 20 mM; RED subdomain of the Sleeping Beauty transposase, [U-13C; U-15N], 2 mg/mL; sodium sulfate 650 mM

sample_conditions_1: ionic strength: 650 mM; pH: 5; pressure: 1 .; temperature: 293 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 HCCH-TOCSY	sample_2	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_2	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

TOPSPIN, Bruker Biospin - collection

xplor-nih, Schwieters, C. D., Kuszewski, J. J., Tjandra, N. and Clore, G. M. - structure calculation

NMR spectrometers:

Bruker AvanceIII 950 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks