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 17653

Title: solution structure of the mSin3A PAH3-SAP30 SID complex   PubMed: 21676866

Deposition date: 2011-05-16 Original release date: 2011-10-26

Authors: Xie, Tao; He, Yuan; Korkeamaki, Hanna; Zhang, Yongbo; Imhoff, Rebecca; Lohi, Olli; Radhakrishnan, Ishwar

Citation: Xie, Tao; He, Yuan; Korkeamaki, Hanna; Zhang, Yongbo; Imhoff, Rebecca; Lohi, Olli; Radhakrishnan, Ishwar. "Structure of the 30-kDa Sin3-associated protein (SAP30) in complex with the mammalian Sin3A corepressor and its role in nucleic acid binding."  J. Biol. Chem. 286, 27814-27824 (2011).

Assembly members:
SAP30, polymer, 94 residues, 10546.846 Da.
entity_2, polymer, 75 residues, 8674.021 Da.

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

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

Entity Sequences (FASTA):
SAP30: SNAGSDDDGGDSPVQDIDTP EVDLYQLQVNTLRRYKRHFK LPTRPGLNKAQLVEIVGCHF KSIPVNEKDTLTCFIYSVRN DKNKSDLKADSGVH
entity_2: SNASKHGVGTESLFFDKVRK ALRSAEAYENFLRCLVIFNQ EVISRAELVQLVSPFLGKFP ELFNWFKNFLGYKES

Data sets:
Data typeCount
13C chemical shifts699
15N chemical shifts174
1H chemical shifts1086

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SAP301
2PAH32

Entities:

Entity 1, SAP30 94 residues - 10546.846 Da.

Residues 1-3 are from non-native tag. This is the SID domain of SAP30 protein.

1   SERASNALAGLYSERASPASPASPGLYGLY
2   ASPSERPROVALGLNASPILEASPTHRPRO
3   GLUVALASPLEUTYRGLNLEUGLNVALASN
4   THRLEUARGARGTYRLYSARGHISPHELYS
5   LEUPROTHRARGPROGLYLEUASNLYSALA
6   GLNLEUVALGLUILEVALGLYCYSHISPHE
7   LYSSERILEPROVALASNGLULYSASPTHR
8   LEUTHRCYSPHEILETYRSERVALARGASN
9   ASPLYSASNLYSSERASPLEULYSALAASP
10   SERGLYVALHIS

Entity 2, PAH3 75 residues - 8674.021 Da.

Residues 1-3 are from non-native tag. This is the PAH3 domain of mSIN3A.

1   SERASNALASERLYSHISGLYVALGLYTHR
2   GLUSERLEUPHEPHEASPLYSVALARGLYS
3   ALALEUARGSERALAGLUALATYRGLUASN
4   PHELEUARGCYSLEUVALILEPHEASNGLN
5   GLUVALILESERARGALAGLULEUVALGLN
6   LEUVALSERPROPHELEUGLYLYSPHEPRO
7   GLULEUPHEASNTRPPHELYSASNPHELEU
8   GLYTYRLYSGLUSER

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 1 mM; entity_2 1 mM; H2O 90%; D2O 10%

sample_2: entity_1 1 mM; entity_2, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%

sample_3: entity_1, [U-100% 13C; U-100% 15N], 1 mM; entity_2 1 mM; D2O 100%

sample_4: entity_1 1 mM; entity_2, [U-100% 13C; U-100% 15N], 1 mM; D2O 100%

sample_conditions_1: pH: 6.5; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_4isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_3isotropicsample_conditions_1
3D HCCH-COSYsample_4isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_4isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_4isotropicsample_conditions_1

Software:

ARIA v1.2, Linge, O, . - structure solution

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

FELIX v98, Accelrys Software Inc. - processing

VNMRJ, Varian - collection

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAB27273 BAC40543 BAD90217
GB AAC26007 AAI32082 AAI32088 EDL28616 EDL28617 AAA69772 AAA69773 AAA89119 AAB01610 AAH52716
REF NP_068560 XP_005607821 XP_006253148 XP_008512731 XP_008770398 NP_001102231 NP_001103820 NP_001103821 NP_035508 XP_001491398
SP O88574 Q60520
TPG DAA17551

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