BMRB Entry 34004

Name: Solution structure of the human SNF5/INI1 domain
Published: 2017-05-04

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PDB ID: 5l7b
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34004
MolProbity Validation Chart

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution structure of the human SNF5/INI1 domain PubMed: 30222246

Deposition date: 2016-06-02 Original release date: 2017-05-04

Authors: Allen, M.; Zinzalla, G.; Bycroft, Mark

Citation: Sammak, Susan; Allen, Mark; Hamdani, Najoua; Bycroft, Mark; Zinzalla, Giovanna. "The structure of INI1/hSNF5 RPT1 and its interactions with the c-MYC:MAX heterodimer provide insights into the interplay between MYC and the SWI/SNF chromatin remodeling complex" FEBS J. 285, 4165-4180 (2018).

Assembly members:
SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1, polymer, 78 residues, 8821.944 Da.

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

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

Entity Sequences (FASTA):
SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1: GGSEVLVPIRLDMEIDGQKL RDAFTWNMNEKLMTPEMFSE ILCDDLDLNPLTFVPAIASA IRQQIESYPTDSILEDQS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	273
15N chemical shifts	77
1H chemical shifts	568

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 78 residues - 8821.944 Da.

1

GLY

SER

GLU

VAL

LEU

VAL

PRO

ILE

ARG

2

LEU

ASP

MET

GLU

ILE

ASP

GLY

GLN

LYS

LEU

3

ARG

ASP

ALA

PHE

THR

TRP

ASN

MET

ASN

GLU

4

LYS

LEU

MET

THR

PRO

GLU

MET

PHE

SER

GLU

5

ILE

LEU

CYS

ASP

LEU

ASP

LEU

ASN

PRO

6

LEU

THR

PHE

VAL

PRO

ALA

ILE

ALA

SER

ALA

7

ILE

ARG

GLN

ILE

GLU

SER

TYR

PRO

THR

8

ASP

SER

ILE

LEU

GLU

ASP

GLN

SER

Samples:

sample_1: beta-mercaptoethanol, [U-100% 2H], 5 mM; potassium phosphate 20 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_2: beta-mercaptoethanol, [U-100% 2H], 5 mM; potassium phosphate 20 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 120 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D DQF-COSY	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNHB	sample_2	isotropic	sample_conditions_1
3D HNCACO	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1

Software:

ANSIG, Kraulis - chemical shift assignment, peak picking

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure calculation

NMR spectrometers:

Bruker Avance 800 MHz
Bruker DRX 600 MHz

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