NMR STRUCTURE OF THE HUMAN MAD1 TRANSREPRESSION DOMAIN SID IN COMPLEX WITH MAMMALIAN SIN3A PAH2 DOMAIN
Solution structure of the interacting domains of the Mad-Sin3 complex: implications for recruitment of a chromatin-modifying complex.
SIN3 INTERACTION DOMAIN (SID) TRANSREPRESSION DOMAIN
PAIRED AMPHIPATHIC HELIX 2 (PAH2 REPEAT)
SLQNNQPVEFNHAINYVNKIKNRFQGQPDIYKAFLEILHTYQKEQRNAKEAGGNYTPALTEQEVYAQVARLFKNQEDLLS EFGQFLPDA
The peptide sequence was synthesized via automated methods. The sequence is naturally found in Homo sapiens (human).
Interproton NOEs were assigned iteratively but manually during structure refinement.
structures with favorable non-bond energy,structures with the least restraint violations
2D Spin-echo Difference for JNCgamma, JC'Cgamma
The structures are based on 1612 unique distance constraints, 198 torsion angle constraints and 72 JHNHA coupling constant constraints.
1.0 mM 1:1 SID unlabeled, PAH2 U-15N; 1.6 mM 1:1 SID unlabeled, PAH2 U-15N, U-13C.
1.6 mM 1:1 SID unlabeled, PAH2 U-15N,13C; 20 mM phosphate buffer pH 6.0, 0.2% NaN3
Four-helix bundle, Protein-peptide Complex, TRANSCRIPTION