BMRB Entry 25599

Name: Solution structure of Sds3 in complex with Sin3A
Published: 2015-07-13

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PDB ID: 2n2h
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25599
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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 Sds3 in complex with Sin3A

Deposition date:

2015-05-08

Original release date:

2015-07-13

Authors:

Clark, Michael; Radhakrishnan, Ishwar

Citation:

Citation: Clark, Michael; Marcum, Ryan; Graveline, Richard; Chan, Clarence; Xie, Tao; Chen, Zhonglei; Ding, Yujia; Zhang, Yongbo; Mondragon, Alfonso; David, Gregory; Radhakrishnan, Ishwar. "Structural Insights into the Assembly of the Histone Deacetylase-Associated Sin3L/Rpd3L Corepressor Complex" Proc. Natl. Acad. Sci. U.S.A. 112, E3669-E3678 (2015).
PubMed: 26124119

Assembly members:

Assembly members:
Sds3SID, polymer, 27 residues, 3125.556 Da.
Sin3HID, polymer, 125 residues, 14698.959 Da.

Natural source:

Natural source: Common Name: house mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pMCSG7

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Sds3SID: SNAAQLNYLLTDEQIMEDLR TLNKLKS
Sin3HID: SNAEHIYRCEDERFELDVVL ETNLATIRVLEAIQKKLSRL SAEEQAKFRLDNTLGGTSEV IHRKALQRIYADKAADIIDG LRKNPSIAVPIVLKRLKMKE EEWREAQRGFNKVWREQNEK YYLKS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2

Data type	Count
13C chemical shifts	631
15N chemical shifts	154
1H chemical shifts	1005

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Sds3SID	1
2	Sin3HID	2

Entities:

Entity 1, Sds3SID 27 residues - 3125.556 Da.

1

SER

ASN

ALA

GLN

LEU

ASN

TYR

LEU

2

THR

ASP

GLU

GLN

ILE

MET

GLU

ASP

LEU

ARG

3

THR

LEU

ASN

LYS

LEU

LYS

SER

Entity 2, Sin3HID 125 residues - 14698.959 Da.

1

SER

ASN

ALA

GLU

HIS

ILE

TYR

ARG

CYS

GLU

2

ASP

GLU

ARG

PHE

GLU

LEU

ASP

VAL

LEU

3

GLU

THR

ASN

LEU

ALA

THR

ILE

ARG

VAL

LEU

4

GLU

ALA

ILE

GLN

LYS

LEU

SER

ARG

LEU

5

SER

ALA

GLU

GLN

ALA

LYS

PHE

ARG

LEU

6

ASP

ASN

THR

LEU

GLY

THR

SER

GLU

VAL

7

ILE

HIS

ARG

LYS

ALA

LEU

GLN

ARG

ILE

TYR

8

ALA

ASP

LYS

ALA

ASP

ILE

ASP

GLY

9

LEU

ARG

LYS

ASN

PRO

SER

ILE

ALA

VAL

PRO

10

ILE

VAL

LEU

LYS

ARG

LEU

LYS

MET

LYS

GLU

11

GLU

TRP

ARG

GLU

ALA

GLN

ARG

GLY

PHE

12

ASN

LYS

VAL

TRP

ARG

GLU

GLN

ASN

GLU

LYS

13

TYR

LEU

LYS

SER

Samples:

sample_1: Sin3HID, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; Sds3SID0.5 – 1 mM; H2O 90%; D2O 10%

sample_2: Sds3SID, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; Sin3HID0.5 – 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.12 M; pH: 6.7; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - structure solution

NMR spectrometers:

Agilent DD2 600 MHz

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