BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 17485

Title: Solution structure of Pf1 SID1-mSin3A PAH2 Complex   PubMed: 21440557

Deposition date: 2011-02-23 Original release date: 2011-03-30

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

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).

Assembly members:
entity_1, polymer, 45 residues, 4993.651 Da.
entity_2, polymer, 94 residues, 10816.996 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):
entity_1: SNADYVQPQLRRPFELLIAA AMERNPTQFQLPNELTCTTA LPGSS
entity_2: SNASLQNNQPVEFNHAINYV NKIKNRFQGQPDIYKAFLEI LHTYQKEQRNAKEAGGNYTP ALTEQEVYAQVARLFKNQED LLSEFGQFLPDANS

Data sets:
Data typeCount
13C chemical shifts545
15N chemical shifts136
1H chemical shifts866

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 45 residues - 4993.651 Da.

1   SERASNALAASPTYRVALGLNPROGLNLEU
2   ARGARGPROPHEGLULEULEUILEALAALA
3   ALAMETGLUARGASNPROTHRGLNPHEGLN
4   LEUPROASNGLULEUTHRCYSTHRTHRALA
5   LEUPROGLYSERSER

Entity 2, entity_2 94 residues - 10816.996 Da.

1   SERASNALASERLEUGLNASNASNGLNPRO
2   VALGLUPHEASNHISALAILEASNTYRVAL
3   ASNLYSILELYSASNARGPHEGLNGLYGLN
4   PROASPILETYRLYSALAPHELEUGLUILE
5   LEUHISTHRTYRGLNLYSGLUGLNARGASN
6   ALALYSGLUALAGLYGLYASNTYRTHRPRO
7   ALALEUTHRGLUGLNGLUVALTYRALAGLN
8   VALALAARGLEUPHELYSASNGLNGLUASP
9   LEULEUSERGLUPHEGLYGLNPHELEUPRO
10   ASPALAASNSER

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:

NameSampleSample stateSample conditions
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Varian Inova 600 MHz

Related Database Links:

BMRB 18000 4635
PDB
DBJ BAD18713 BAE00370 BAE24837 BAE33212 BAE41602
GB AAH01657 AAH43080 AAI10883 AAI21044 AAI21045 AAK95854
REF NP_001013135 NP_001028733 NP_001179060 NP_001253214 NP_001277060 XP_004660420 XP_005994973 XP_007239639 XP_009197516
SP Q5SPL2 Q96QT6
TPG DAA18992

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