BMRB Entry 15569

Name: SOLUTION STRUCTURE OF MSIN3A PAH1 DOMAIN
Published: 2008-06-27

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR15569

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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 MSIN3A PAH1 DOMAIN

Deposition date:

2007-11-27

Original release date:

2008-06-27

Authors:

Sahu, S.; Swanson, K.; Kang, R.; Huang, K.; Brubaker, K.; Ratcliff, K.; Radhakrishnan, I.

Citation:

Citation: Sahu, S.; Swanson, K.; Kang, R.; Huang, K.; Brubaker, K.; Ratcliff, K.; Radhakrishnan, I.. "Conserved themes in target recognition by the PAH1 and PAH2 domains of the Sin3 transcriptional corepressor" J. Mol. Biol. 375, 1444-1456 (2008).
PubMed: 18089292

Assembly members:

Assembly members:
PAIRED_AMPHIPATHIC_HELIX_PROTEIN_SIN3A, polymer, 71 residues, 8087.342 Da.

Natural source:

Natural source: Common Name: 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: PET30

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PAIRED_AMPHIPATHIC_HELIX_PROTEIN_SIN3A: QRLKVEDALSYLDQVKLQFG SQPQVYNDFLDIMKEFKSQS IDTPGVISRVSQLFKGHPDL IMGFNTFLPPG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	321
15N chemical shifts	74
1H chemical shifts	480

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PAH1	1

Entities:

Entity 1, PAH1 71 residues - 8087.342 Da.

1

GLN

ARG

LEU

LYS

VAL

GLU

ASP

ALA

LEU

SER

2

TYR

LEU

ASP

GLN

VAL

LYS

LEU

GLN

PHE

GLY

3

SER

GLN

PRO

GLN

VAL

TYR

ASN

ASP

PHE

LEU

4

ASP

ILE

MET

LYS

GLU

PHE

LYS

SER

GLN

SER

5

ILE

ASP

THR

PRO

GLY

VAL

ILE

SER

ARG

VAL

6

SER

GLN

LEU

PHE

LYS

GLY

HIS

PRO

ASP

LEU

7

ILE

MET

GLY

PHE

ASN

THR

PHE

LEU

PRO

8

GLY

Samples:

sample_1: PAH1, [U-100% 15N], 1 mM; SODIUM PHOSPHATE 20 mM; SODIUM AZIDE 0.2%; DTT 2 mM; D2O, [U-100% 2H], 10%; H2O 90%

sample)_2: PAH1, [U-100% 13C; U-100% 15N], 1 mM; SODIUM PHOSPHATE 20 mM; SODIUM AZIDE 0.2%; DTT 2 mM; D2O, [U-100% 2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 0.02 M; pH: 6; pressure: 1 atm; temperature: 288 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

Software:

CNS v1.2, BRUNGER, ADAMS, CLORE, GROS, NILGES, READ - refinement

FELIX v98.0, Accelrys Software Inc. - data analysis

ARIA v1.2, Linge, O'Donoghue and Nilges - structure solution

VNMR, Varian - collection

NMR spectrometers:

VARIAN INOVA 600 MHz

BMRB	15570
PDB	2RMR 2RMS
EMBL	CDQ82228
GB	AAH81027 ETE65880
REF	NP_001129640 XP_012362542 XP_013921538