BMRB: 4841

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

Authors

Spronk, C.A.E.M., Jansen, J.F.A., Tessari, M., Kaan, A.M., Aelen, J., Lasonder, E., Stunnenberg, H.G., Vuister, G.W.

Assembly

mSin3B-PAH2 complexed to Mad1

Entity

1. mSin3B-PAH2 domain (polymer, Thiol state: not present), 105 monomers, 12193.36 Da Detail

ESDSVEFNNA ISYVNKIKTR FLDHPEIYRS FLEILHTYQK EQLHTKGRPF RGMSEEEVFT EVANLFRGQE DLLSEFGQFL PEAKRSLFTG NGSAEMNSGQ KNEEK

2. Sin interaction domain of human Mad1 (polymer, Thiol state: not present), 13 monomers, 1522.718 Da Detail

NIQMLLEAAD YLE

Total weight

13716.078 Da

Max. entity weight

12193.36 Da

Source organism

Mus musculus , Homo sapiens

Exptl. method

NMR

Refine. method

SIMULATED ANNEALING, ITERATIVE NOE-ASSIGNMENT

Data set

assigned_chemical_shifts

Chem. Shift Complete1

Sequence coverage: 89.0 %, Completeness: 83.6 %, Completeness (bb): 88.5 % Detail

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Polymer type: polypeptide(L)

	Total	1H	13C	15N
All	83.6 % (1187 of 1420)	84.8 % (632 of 745)	80.8 % (441 of 546)	88.4 % (114 of 129)
Backbone	88.5 % (621 of 702)	89.2 % (214 of 240)	87.9 % (305 of 347)	88.7 % (102 of 115)
Sidechain	80.1 % (664 of 829)	82.8 % (418 of 505)	75.5 % (234 of 310)	85.7 % (12 of 14)
Aromatic	53.0 % (71 of 134)	67.2 % (45 of 67)	38.8 % (26 of 67)
Methyl	81.1 % (86 of 106)	81.1 % (43 of 53)	81.1 % (43 of 53)

1. mSin3B-PAH2 domain

ESDSVEFNNA ISYVNKIKTR FLDHPEIYRS FLEILHTYQK EQLHTKGRPF RGMSEEEVFT EVANLFRGQE DLLSEFGQFL PEAKRSLFTG NGSAEMNSGQ KNEEK

2. Sin interaction domain of human Mad1

NIQMLLEAAD YLE

Show sample condition

Sample

Temperature 293 (±1) K, pH 6.3 (±0.1), Details Trace amounts of Sodium azide and protease inhibitors were added for conservation

#	Name	Isotope labeling	Type	Concentration
1	mSin3B-PAH2 domain	[U-100% 13C; U-100% 15N]		1.0 mM
2	Sin interaction domain of human Mad1			1.0 mM
3	Potassium_Phosphate			50 mM
4	NaN3			0.0 ~ 0.0 mM
5	protease inhibitors			0.0 ~ 0.0 mM

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Chem. Shift Complete2

Sequence coverage: 33.1 %, Completeness: 50.3 %, Completeness (bb): 54.3 % Detail

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Polymer type: polypeptide(L)

	Total	1H	13C	15N
All	50.3 % (1428 of 2840)	53.3 % (794 of 1490)	45.3 % (495 of 1092)	53.9 % (139 of 258)
Backbone	54.3 % (763 of 1404)	58.7 % (282 of 480)	51.2 % (355 of 694)	54.8 % (126 of 230)
Sidechain	47.3 % (784 of 1658)	50.7 % (512 of 1010)	41.8 % (259 of 620)	46.4 % (13 of 28)
Aromatic	28.0 % (75 of 268)	36.6 % (49 of 134)	19.4 % (26 of 134)
Methyl	47.2 % (100 of 212)	53.8 % (57 of 106)	40.6 % (43 of 106)

1. mSin3B-PAH2 domain

ESDSVEFNNA ISYVNKIKTR FLDHPEIYRS FLEILHTYQK EQLHTKGRPF RGMSEEEVFT EVANLFRGQE DLLSEFGQFL PEAKRSLFTG NGSAEMNSGQ KNEEK

2. Sin interaction domain of human Mad1

NIQMLLEAAD YLE

Show sample condition

Sample

Temperature 293 (±1) K, pH 6.3 (±0.1), Details Trace amounts of Sodium azide and protease inhibitors were added for conservation

#	Name	Isotope labeling	Type	Concentration
1	mSin3B-PAH2 domain	[U-100% 13C; U-100% 15N]		1.0 mM
2	Sin interaction domain of human Mad1			1.0 mM
3	Potassium_Phosphate			50 mM
4	NaN3			0.0 ~ 0.0 mM
5	protease inhibitors			0.0 ~ 0.0 mM

Hide sample codition

Protein Blocks Logo

Calculated from 20 models in PDB: 1E91, Strand ID: A, B Detail

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Release date

2001-04-25

Citation 1

Sequence-specific assignment of the PAH2 domain of Sin3B free and bound to Mad1
Spronk, C.A.E.M., Jansen, J.F.A., Tessari, M., Kaan, A.M., Aelen, J., Lasonder, E., Stunnenberg, H.G., Vuister, G.W.
J. Biomol. NMR (2001), 19, 377-378, PubMed 11370785 , Abstract

Show more 3 citaions

Citation 2

NMRPipe: a multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., Bax, A.
J. Biomol. NMR (1995), 6, 277-293, PubMed 8520220 , Abstract

Citation 3

Crystallography & NMR system: A new software suite for macromolecular structure determination
Brunger, A.T., Adams, P.D., Clore, G.M., DeLano, W.L., Gros, P., Grosse-Kunstleve, R.W., Jiang, J.S., Kuszewski, J., Nilges, M., Pannu, N.S., Read, R.J., Rice, L.M., Simonson, T., Warren, G.L.
Acta Crystallogr. D. Biol. Crystallogr. (1998), 54, 905-921, PubMed 9757107 , DOI: , Abstract

Citation 4

Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from beta-spectrin
Nilges, M., Macias, M.J., O'Donoghue, S.I., Oschkinat, H.
J. Mol. Biol. (1997), 269, 408-422, PubMed 9199409 , DOI 10.1006/jmbi.1997.1044 , Abstract

Hide non-primary 3 citaions

Related entities 1. mSin3B-PAH2 domain, : 3 : 32 entities Detail

Related entities 2. Sin interaction domain of human Mad1, : 1 : 5 : 5 : 1 entities Detail

Interaction partners 1. mSin3B-PAH2 domain, : 9 interactors Detail

Interaction partners 2. Sin interaction domain of human Mad1, : 6 : 1 interactors Detail

Experiments performed 16 experiments Detail