BMRB: 10041

Solution Structure of the Tudor Domain from Mouse Hypothetical Protein Homologous to Histone Acetyltransferase

Authors

Li, H., Saito, K., Koshiba, S., Inoue, M., Kigawa, T., Yokoyama, S.

Assembly

MYST histone acetyltransferase 1

Entity

1. MYST histone acetyltransferase 1 (polymer, Thiol state: all free), 133 monomers, 15211.50 Da Detail

GSSGSSGEPE VTVEIGETYL CRRPDSTWHS AEVIQSRVND QEGREEFYVH YVGFNRRLDE WVDKNRLALT KTVKDAVQKN SEKYLSELAE QPERKITRNQ KRKHDEINHV QKTYAEMDPT TAALEKESGP SSG

Formula weight

15211.5 Da

Source organism

Mus musculus

Exptl. method

NMR

Refine. method

torsion angle dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 89.5 %, Completeness: 84.4 %, Completeness (bb): 85.4 % Detail

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Polymer type: polypeptide(L)

	Total	1H	13C	15N
All	84.4 % (1297 of 1536)	82.4 % (666 of 808)	87.7 % (514 of 586)	82.4 % (117 of 142)
Backbone	85.4 % (673 of 788)	83.3 % (224 of 269)	87.2 % (341 of 391)	84.4 % (108 of 128)
Sidechain	82.8 % (723 of 873)	80.7 % (435 of 539)	87.2 % (279 of 320)	64.3 % (9 of 14)
Aromatic	92.0 % (92 of 100)	92.0 % (46 of 50)	91.7 % (44 of 48)	100.0 % (2 of 2)
Methyl	93.1 % (108 of 116)	93.1 % (54 of 58)	93.1 % (54 of 58)

1. Tudor domain

GSSGSSGEPE VTVEIGETYL CRRPDSTWHS AEVIQSRVND QEGREEFYVH YVGFNRRLDE WVDKNRLALT KTVKDAVQKN SEKYLSELAE QPERKITRNQ KRKHDEINHV QKTYAEMDPT TAALEKESGP SSG

Show sample condition

Sample

Pressure 1 (±0.001) atm, Temperature 298 (±0.1) K, pH 7.0 (±0.05)

#	Name	Isotope labeling	Type	Concentration
1	Tudor domain	[U-13C, U-15N]		1.06 mM
2	d-Tris-HCl		buffer	20 mM
3	NaCl		salt	100 mM
4	d-DTT		salt	1 mM
5	NaN3			0.02 %
6	H2O		solvent	90 %
7	D2O		solvent	10 %

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LACS Plot; CA

Referencing offset: -0.16 ppm, Outliers: 1 Detail

Show chemical shift referencing parameters

Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
1H	DSS	methyl protons	0.0 ppm	null	indirect	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

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LACS Plot; CB

Referencing offset: -0.16 ppm, Outliers: 1 Detail

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Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
1H	DSS	methyl protons	0.0 ppm	null	indirect	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

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LACS Plot; HA

Referencing offset: 0.01 ppm, Outliers: 3 Detail

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Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
1H	DSS	methyl protons	0.0 ppm	null	indirect	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

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LACS Plot; CO

Referencing offset: 0.16 ppm, Outliers: 1 Detail

Show chemical shift referencing parameters

Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
1H	DSS	methyl protons	0.0 ppm	null	indirect	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

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Protein Blocks Logo

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

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Release date

2008-08-12

Citation

Solution Structure of the Tudor Domain from Mouse Hypothetical Protein Homologous to Histone Acetyltransferase
Li, H., Saito, K., Koshiba, S., Inoue, M., Kigawa, T., Yokoyama, S.

Related entities 1. MYST histone acetyltransferase 1, : 1 : 7 : 8 entities Detail

Interaction partners 1. MYST histone acetyltransferase 1, : 13 interactors Detail

Experiments performed 2 experiments Detail