BMRB Entry 17485

Name: Solution structure of Pf1 SID1-mSin3A PAH2 Complex
Published: 2011-03-30

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PDB ID: 2l9s
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17485
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of Pf1 SID1-mSin3A PAH2 Complex

Deposition date:

2011-02-23

Original release date:

2011-03-30

Authors:

Senthil Kumar, Ganesan; Xie, Tao; Zhang, Yongbo; Radhakrishnan, Ishwar

Citation:

Citation: Kumar, Ganesan Senthil; Xie, Tao; Zhang, Yongbo; Radhakrishnan, Ishwar. "Solution Structure of the mSin3A PAH2-Pf1 SID1 Complex: A Mad1/Mxd1-Like Interaction Disrupted by MRG15 in the Rpd3S/Sin3S Complex." J. Mol. Biol. 408, 987-1000 (2011).
PubMed: 21440557

Assembly members:

Assembly members:
entity_1, polymer, 45 residues, 4993.651 Da.
entity_2, polymer, 94 residues, 10816.996 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: pMCSG7

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SNADYVQPQLRRPFELLIAA AMERNPTQFQLPNELTCTTA LPGSS
entity_2: SNASLQNNQPVEFNHAINYV NKIKNRFQGQPDIYKAFLEI LHTYQKEQRNAKEAGGNYTP ALTEQEVYAQVARLFKNQED LLSEFGQFLPDANS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	545
15N chemical shifts	136
1H chemical shifts	866

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	2

Entities:

Entity 1, entity_1 45 residues - 4993.651 Da.

1

SER

ASN

ALA

ASP

TYR

VAL

GLN

PRO

GLN

LEU

2

ARG

PRO

PHE

GLU

LEU

ILE

ALA

3

ALA

MET

GLU

ARG

ASN

PRO

THR

GLN

PHE

GLN

4

LEU

PRO

ASN

GLU

LEU

THR

CYS

THR

ALA

5

LEU

PRO

GLY

SER

Entity 2, entity_2 94 residues - 10816.996 Da.

1

SER

ASN

ALA

SER

LEU

GLN

ASN

GLN

PRO

2

VAL

GLU

PHE

ASN

HIS

ALA

ILE

ASN

TYR

VAL

3

ASN

LYS

ILE

LYS

ASN

ARG

PHE

GLN

GLY

GLN

4

PRO

ASP

ILE

TYR

LYS

ALA

PHE

LEU

GLU

ILE

5

LEU

HIS

THR

TYR

GLN

LYS

GLU

GLN

ARG

ASN

6

ALA

LYS

GLU

ALA

GLY

ASN

TYR

THR

PRO

7

ALA

LEU

THR

GLU

GLN

GLU

VAL

TYR

ALA

GLN

8

VAL

ALA

ARG

LEU

PHE

LYS

ASN

GLN

GLU

ASP

9

LEU

SER

GLU

PHE

GLY

GLN

PHE

LEU

PRO

10

ASP

ALA

ASN

SER

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.75 – 1.7 mM; entity_2, [U-100% 13C; U-100% 15N], 0.75 – 1.7 mM; H2O, [U-100% 13C; U-100% 15N], 90%; D2O, [U-100% 13C; U-100% 15N], 10%

sample_conditions_1: ionic strength: 0 M; pH: 6.00; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1

Software:

ARIA v1.2, Brunger, Adams, Clore, Gros, Nilges and Read, Linge, O'Donoghue and Nilges - refinement, structure solution

NMR spectrometers:

Varian Inova 600 MHz

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