BMRB Entry 25307

Name: solution structure of SATB1 homeodomain
Published: 2015-11-02

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PDB ID: 2mw8
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25307
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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:

solution structure of SATB1 homeodomain

Deposition date:

2014-10-31

Original release date:

2015-11-02

Authors:

Yamasaki, Kazuhiko; Yamasaki, Tomoko

Citation:

Citation: Yamasaki, Kazuhiko; Yamasaki, Tomoko. "The combination of sequence-specific and nonspecific DNA-binding modes of transcription factor SATB1" Biochem. J. 473, 3321-3339 (2016).
PubMed: 27462121

Assembly members:

Assembly members:
SATB1, polymer, 71 residues, 7903.208 Da.

Natural source:

Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SATB1: GSHMNRQKTRPRTKISVEAL GILQSFIQDVGLYPDEEAIQ TLSAQLDLPKYTIIKFFQNQ RYYLKHHGKLK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	73
1H chemical shifts	82

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SATB1 homeodomain	1

Entities:

Entity 1, SATB1 homeodomain 71 residues - 7903.208 Da.

1

GLY

SER

HIS

MET

ASN

ARG

GLN

LYS

THR

ARG

2

PRO

ARG

THR

LYS

ILE

SER

VAL

GLU

ALA

LEU

3

GLY

ILE

LEU

GLN

SER

PHE

ILE

GLN

ASP

VAL

4

GLY

LEU

TYR

PRO

ASP

GLU

ALA

ILE

GLN

5

THR

LEU

SER

ALA

GLN

LEU

ASP

LEU

PRO

LYS

6

TYR

THR

ILE

LYS

PHE

GLN

ASN

GLN

7

ARG

TYR

LEU

LYS

HIS

GLY

LYS

LEU

8

LYS

Samples:

sample_1: SATB1 homeodomain, [U-15N], 0.3 mM; sodium phosphate 50 mM; sodium chloride 50 mM; DSS 0.5 mM; H2O 95%; D2O 5%

sample_2: SATB1 homeodomain, [U-15N], 0.7 – 1.2 mM; sodium phosphate 50 mM; sodium chloride 200 mM; DSS 0.5 mM; H2O 90%; D2O 5%

sample_3: SATB1 homeodomain, [U-15N], 0.7 – 1.2 mM; sodium phosphate 50 mM; sodium chloride 200 mM; DSS 0.5 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.1 M; pH: 5.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.25 M; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_2
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_2
3D 1H-15N TOCSY	sample_2	isotropic	sample_conditions_2
2D 1H-1H NOESY	sample_3	isotropic	sample_conditions_2
2D DQF-COSY	sample_3	isotropic	sample_conditions_2
2D 1H-1H TOCSY	sample_3	isotropic	sample_conditions_2

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

Felix, Accelrys Software Inc. - data analysis

NMR spectrometers:

Bruker Avance 500 MHz
Bruker DMX 750 MHz
Bruker DMX 500 MHz

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