BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 4841

Title: 1H, 15N and 13C chemical shift assignments for the PAH2 domain of mSin3B complexed to Mad1-SID   PubMed: 11370785

Authors: Spronk, Christian; Jansen, Jacobus; Tessari, Marco; Kaan, Anita; Aelen, Jan; Lasonder, Edwin; Stunnenberg, Hendrik; Vuister, Geerten

Citation: Spronk, Christian; Jansen, Jacobus; Tessari, Marco; Kaan, Anita; Aelen, Jan; Lasonder, Edwin; Stunnenberg, Hendrik; Vuister, Geerten. "Letter to the Editor: Sequence-specific Assignment of the PAH2 Domain of Sin3B free and bound to Mad1"  J. Biomol. NMR 19, 377-378 (2001).

Assembly members:
mSin3B-PAH2 domain, polymer, 105 residues, Formula weight is not available
Sin interaction domain of human Mad1, polymer, 13 residues, Formula weight is not available

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):
mSin3B-PAH2 domain: ESDSVEFNNAISYVNKIKTR FLDHPEIYRSFLEILHTYQK EQLHTKGRPFRGMSEEEVFT EVANLFRGQEDLLSEFGQFL PEAKRSLFTGNGSAEMNSGQ KNEEK
Sin interaction domain of human Mad1: NIQMLLEAADYLE

Data sets:
Data typeCount
15N chemical shifts114
1H chemical shifts816
13C chemical shifts439

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PAH21
2Mad12

Entities:

Entity 1, PAH2 105 residues - Formula weight is not available

1   GLUSERASPSERVALGLUPHEASNASNALA
2   ILESERTYRVALASNLYSILELYSTHRARG
3   PHELEUASPHISPROGLUILETYRARGSER
4   PHELEUGLUILELEUHISTHRTYRGLNLYS
5   GLUGLNLEUHISTHRLYSGLYARGPROPHE
6   ARGGLYMETSERGLUGLUGLUVALPHETHR
7   GLUVALALAASNLEUPHEARGGLYGLNGLU
8   ASPLEULEUSERGLUPHEGLYGLNPHELEU
9   PROGLUALALYSARGSERLEUPHETHRGLY
10   ASNGLYSERALAGLUMETASNSERGLYGLN
11   LYSASNGLUGLULYS

Entity 2, Mad1 13 residues - Formula weight is not available

1   ASNILEGLNMETLEULEUGLUALAALAASP
2   TYRLEUGLU

Samples:

Typical_sample: mSin3B-PAH2 domain, [U-100% 13C; U-100% 15N], 1.0 mM; Sin interaction domain of human Mad1 1.0 mM; Potassium_Phosphate 50 mM; NaN3 mM; protease inhibitors mM

sample_conditions: pH: 6.3; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
13C-NOESY-HSQCTypical_samplenot availablesample_conditions
15N-NOESY-HSQCTypical_samplenot availablesample_conditions
15N-HMQC-NOESY-HSQCTypical_samplenot availablesample_conditions
(13C-FILTERED)-NOESY-(13C-EDITED)-HSQCTypical_samplenot availablesample_conditions
HNCATypical_samplenot availablesample_conditions
HNCOTypical_samplenot availablesample_conditions
HN(CO)CATypical_samplenot availablesample_conditions
CBCA(CO)NNHTypical_samplenot availablesample_conditions
HNCACBTypical_samplenot availablesample_conditions
(H)CCH-TOCSYTypical_samplenot availablesample_conditions
15N-HSQCTypical_samplenot availablesample_conditions
13C-HSQCTypical_samplenot availablesample_conditions
(13C/15N-FILTERED)-NOESYTypical_samplenot availablesample_conditions
(13C/15N-FILTERED)-TOCSYTypical_samplenot availablesample_conditions
HNHATypical_samplenot availablesample_conditions
HBHA(CBCACO)NNHTypical_samplenot availablesample_conditions

Software:

NMRPipe v1.7 - Data processing

XEASY v1.3.9 - Spectral analysis

CNS v1.0 - structure calculations

ARIA v1.0 - structure calculations and iterative NOE-assignment

NMR spectrometers:

  • Varian Inova 500 MHz
  • Varian Inova 750 MHz
  • Bruker DRX 600 MHz

Related Database Links:

GenBank EDL90864 EDL90863 EDL10815 AAH51536
PDB
BMRB 6899 5808 5457 4874