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Solution structure of the knotted tudor domain of the yeast histone acetyltransferase protein, Esa1
Authors
Shimojo, H., Sano, N., Moriwaki, Y., Okuda, M., Horikoshi, M., Nishimura, Y.
Assembly
the knotted tudor domain
Entity
1. the knotted tudor domain (polymer, Thiol state: all free), 92 monomers, 10773.08 Da Detail

GSHMSHDGKE EPGIAKKINS VDDIIIKCQC WVQKNDEERL AEILSINTRK APPKFYVHYV NYNKRLDEWI TTDRINLDKE VLYPKLKATD ED


Formula weight
10773.08 Da
Source organism
Saccharomyces cerevisiae
Exptl. method
solution NMR
Refine. method
TORSION ANGLE DYNAMICS
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 96.7 %, Completeness (bb): 95.4 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All96.7 % (1078 of 1115)96.9 % (569 of 587)97.0 % (417 of 430)93.9 % (92 of 98)
Backbone95.4 % (519 of 544)95.6 % (175 of 183)95.6 % (261 of 273)94.3 % (83 of 88)
Sidechain97.7 % (645 of 660)97.5 % (394 of 404)98.4 % (242 of 246)90.0 % (9 of 10)
Aromatic100.0 % (78 of 78)100.0 % (39 of 39)100.0 % (37 of 37)100.0 % (2 of 2)
Methyl100.0 % (96 of 96)100.0 % (48 of 48)100.0 % (48 of 48)

1. Residues 1-89

GSHMSHDGKE EPGIAKKINS VDDIIIKCQC WVQKNDEERL AEILSINTRK APPKFYVHYV NYNKRLDEWI TTDRINLDKE VLYPKLKATD ED

Sample #1

Solvent system 95% H2O/5% D2O, Pressure 1 atm, Temperature 295 K, pH 6.8


#NameIsotope labelingTypeConcentration
1Residues 1-89[U-99% 13C; U-99% 15N]0.35 mM
2potassium phosphate200 mM
3H2O95 %
4D2O5 %
Sample #2

Solvent system 100% D2O, Pressure 1 atm, Temperature 295 K, pH 6.8


#NameIsotope labelingTypeConcentration
5Residues 1-89natural abundance0.35 mM
6potassium phosphate200 mM
7D2O100 %

LACS Plot; CA
Referencing offset: 0.12 ppm, Outliers: 2 Detail
LACS Plot; CB
Referencing offset: 0.12 ppm, Outliers: 2 Detail
LACS Plot; HA
Referencing offset: -0.06 ppm, Outliers: 1 Detail
LACS Plot; CO
Referencing offset: 0.37 ppm, Outliers: 3 Detail
Protein Blocks Logo
Calculated from 20 models in PDB: 2RO0, Strand ID: A Detail


Release date
2008-04-15
Citation
Novel structural and functional mode of a knot essential for RNA binding activity of the Esa1 presumed chromodomain
Shimojo, H., Sano, N., Moriwaki, Y., Okuda, M., Horikoshi, M., Nishimura, Y.
J. Mol. Biol. (2008), 378, 987-1001, PubMed 18407291 , DOI 10.1016/j.jmb.2008.03.021 ,
Entries sharing articles BMRB: 1 entries Detail
  BMRB: 11033 released on 2008-04-15
    Title Solution structure of the presumed chromodomain of the yeast histone acetyltransferase protein, Esa1
Related entities 1. the knotted tudor domain, : 1 : 2 : 12 entities Detail
Interaction partners 1. the knotted tudor domain, : 42 interactors Detail
Experiments performed 10 experiments Detail
nullKeywords chromodomain, Esa1, HAT, RNA binding, tudor domain