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BMRB: 30585


30585
6O7G
Solution structure of MLL4 PHD6 domain in complex with histone H4K16ac peptide
Authors
Zhang, Y., Kutateladze, T.G.
Assembly
Histone-lysine N-methyltransferase 2D (E.C.2.1.1.43), Histone H4
Entity
1. Histone-lysine N-methyltransferase 2D (E.C.2.1.1.43), Histone H4, entity 1 (polymer, Thiol state: all other bound), 64 monomers, 7233.089 Da Detail

GSHMSLVTCP ICHAPYVEED LLIQCRHCER WMHAGCESLF TEDDVEQAAD EGFDCVSCQP YVVK


2. Histone-lysine N-methyltransferase 2D (E.C.2.1.1.43), Histone H4, entity 2 (polymer, Thiol state: not present), 13 monomers, 1259.487 Da Detail

XGKGGAXRHR KVX


3. Histone-lysine N-methyltransferase 2D (E.C.2.1.1.43), Histone H4, entity ZN (non-polymer), 65.409 × 2 Da
Total weight
8623.395 Da
Max. entity weight
7233.089 Da
Entity Connection
na 8 Detail
IDTypeValue orderAtom ID 1Atom ID 2
1nasing1:CYS9:SG3:ZN1:ZN
2nasing1:CYS12:SG3:ZN1:ZN
3nasing1:HIS33:ND13:ZN1:ZN
4nasing1:CYS36:SG3:ZN1:ZN
5nasing1:CYS25:SG3:ZN1:ZN
6nasing1:CYS28:SG3:ZN1:ZN
7nasing1:CYS55:SG3:ZN1:ZN
8nasing1:CYS58:SG3:ZN1:ZN

Source organism
Homo sapiens
Exptl. method
solution NMR
Refine. method
simulated annealing
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 84.4 %, Completeness: 75.1 %, Completeness (bb): 74.4 % Detail
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Polymer type: polypeptide(L)

Total1H13C15N
All75.1 % (614 of 818)77.8 % (329 of 423)70.6 % (226 of 320)78.7 % (59 of 75)
Backbone74.4 % (326 of 438)80.1 % (121 of 151)69.4 % (150 of 216)77.5 % (55 of 71)
Sidechain76.8 % (344 of 448)76.5 % (208 of 272)76.7 % (132 of 172)100.0 % (4 of 4)
Aromatic70.6 % (48 of 68)82.4 % (28 of 34)57.6 % (19 of 33)100.0 % (1 of 1)
Methyl86.4 % (57 of 66)84.8 % (28 of 33)87.9 % (29 of 33)

1. entity 1

GSHMSLVTCP ICHAPYVEED LLIQCRHCER WMHAGCESLF TEDDVEQAAD EGFDCVSCQP YVVK

2. entity 2

XGKGGAXRHR KVX

Show sample condition
Sample

Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 298 K, pH 7.0, Details 2.5 mM [U-13C; U-15N] MLL4 PHD6, 7.5 mM histone H4K16ac (11-21) peptide, 93% H2O/7% D2O


#NameIsotope labelingTypeConcentration
1MLL4 PHD6[U-13C; U-15N]2.5 mM
2histone H4K16ac (11-21) peptidenatural abundance7.5 mM
3NaCl buffernatural abundance100 mM

Protein Blocks Logo
Calculated from 15 models in PDB: 6O7G, Strand ID: A, B Detail

Release date
2019-05-15
Citation
Selective binding of the PHD6 finger of MLL4 to histone H4K16ac links MLL4 and MOF
Zhang, Y., Jang, Y., Lee, J.E., Ahn, J.W., Xu, L., Holden, M.R., Cornett, E.M., Krajewski, K., Klein, B.J., Wang, S.P., Dou, Y., Roeder, R.G., Strahl, B.D., Rothbart, S.B., Shi, X., Ge, K., Kutateladze, T.G.
Nat. Commun. (2019), 10, 2314-2314, PubMed 31127101 , DOI 10.1038/s41467-019-10324-8 ,
Related entities 1. Histone-lysine N-methyltransferase 2D (E.C.2.1.1.43), Histone H4, entity 1, : 1 : 1 : 48 entities Detail
More details for 50 related entities
Experiments performed 9 experiments Detail
nullKeywords H4K16ac, MLL4, MOF, PHD finger, TRANSCRIPTION, acetylation, chromatin, histone