BMRB Entry 15570

Name: SOLUTION STRUCTURE OF THE MSIN3A PAH1-SAP25 SID COMPLEX
Published: 2008-06-27

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15570

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

SOLUTION STRUCTURE OF THE MSIN3A PAH1-SAP25 SID COMPLEX

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.
Sap25, polymer, 61 residues, Formula weight is not available

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
Sap25: SSTWLSEAEMIALAGLLQMS QGEQTPNCVASSLPSTSCPD PVSVSEDPGPSGDQSCSGTD T

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	548
15N chemical shifts	127
1H chemical shifts	791

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PAH1	1
2	Sap25	2

Entities:

Entity 1, PAH1 71 residues - 8087.342 Da.

119-189:PAH1 127-186:Sap25

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

Entity 2, Sap25 61 residues - Formula weight is not available

In the chemical shift table it starts after PAH1 residues 119-189

1

SER

THR

TRP

LEU

SER

GLU

ALA

GLU

MET

2

ILE

ALA

LEU

ALA

GLY

LEU

GLN

MET

SER

3

GLN

GLY

GLU

GLN

THR

PRO

ASN

CYS

VAL

ALA

4

SER

LEU

PRO

SER

THR

SER

CYS

PRO

ASP

5

PRO

VAL

SER

VAL

SER

GLU

ASP

PRO

GLY

PRO

6

SER

GLY

ASP

GLN

SER

CYS

SER

GLY

THR

ASP

7

THR

Samples:

sample_1: Sap25, [U-100% 15N], 1 mM; 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: 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

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	15569
PDB	2RMR 2RMS 2RMS
EMBL	CDQ82228 CAK36853
GB	AAH81027 ETE65880 AAI52783 AAI56602
REF	NP_001129640 XP_012362542 XP_013921538 NP_001075431
SP	Q1EHW4
AlphaFold	Q1EHW4