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1H and 15N assignment of SMRT DAD
Authors
Codina, A., Schwabe, J.W.R.
Assembly
SMRT deacetylase activation domain
Entity
1. SMRT deacetylase activation domain (polymer, Thiol state: not present), 68 monomers, 8290.525 Da Detail

NGLMADPMKV YKDRQVMNMW SEQEKETFRE KFMQHPKNFG LIASFLERKT VAECVLYYYL TKKNENYK


Formula weight
8290.525 Da
Source organism
Homo sapiens
Exptl. method
NMR
Refine. method
Simulated annealing protocol
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 98.5 %, Completeness: 80.3 %, Completeness (bb): 96.5 % Detail

Polymer type: polypeptide(L)

Total1H15N
All80.3 % (432 of 538)77.8 % (360 of 463)96.0 % (72 of 75)
Backbone96.5 % (195 of 202)96.3 % (131 of 136)97.0 % (64 of 66)
Sidechain70.5 % (237 of 336)70.0 % (229 of 327)88.9 % (8 of 9)
Aromatic57.1 % (28 of 49)58.3 % (28 of 48) 0.0 % (0 of 1)
Methyl92.3 % (24 of 26)92.3 % (24 of 26)

1. SMRT deacetylase activation domain

NGLMADPMKV YKDRQVMNMW SEQEKETFRE KFMQHPKNFG LIASFLERKT VAECVLYYYL TKKNENYK

Sample #1

Temperature 290 (±1) K, pH 6.8 (±0.1)


#NameIsotope labelingTypeConcentration
1SMRT deacetylase activation domain1.0 ~ 2.0 mM
2NaCl50 mM
3sodium phosphate50 mM
Sample #2

Temperature 290 (±1) K, pH 6.8 (±0.1)


#NameIsotope labelingTypeConcentration
4SMRT deacetylase activation domain[U-15N]1.0 ~ 2.0 mM
5NaCl50 mM
6sodium phosphate50 mM

Protein Blocks Logo
Calculated from 28 models in PDB: 1XC5, Strand ID: A Detail


Release date
2005-06-01
Citation
Structural insights into the interaction and activation of histone deacetylase 3 by nuclear receptor corepressors
Codina, A., Love, J.D., Li, Y., Lazar, M.A., Neuhaus, D., Schwabe, J.W.R.
Proc. Natl. Acad. Sci. U. S. A. (2005), 102, 6009-6014, PubMed 15837933 , DOI 10.1073/pnas.0500299102 ,
Related entities 1. SMRT deacetylase activation domain, : 1 : 3 : 33 entities Detail
Interaction partners 1. SMRT deacetylase activation domain, : 40 interactors Detail
Experiments performed 7 experiments Detail
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