BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 30585

Title: Solution structure of MLL4 PHD6 domain in complex with histone H4K16ac peptide   PubMed: 31127101

Deposition date: 2019-03-07 Original release date: 2019-05-17

Authors: Zhang, Y.; Kutateladze, T.

Citation: Zhang, Y.; Jang, Y.; Lee, J.; Ahn, J.; Xu, L.; Holden, M.; Cornett, E.; Krajewski, K.; Klein, B.; Wang, S.; Dou, Y.; Roeder, R.; Strahl, B.; Rothbart, S.; Shi, X.; Ge, K.; Kutateladze, T.. "Selective binding of the PHD6 finger of MLL4 to histone H4K16ac links MLL4 and MOF"  Nat. Commun. 10, 2314-2314 (2019).

Assembly members:
entity_1, polymer, 64 residues, 7240.149 Da.
entity_2, polymer, 13 residues, 1264.527 Da.
entity_ZN, non-polymer, 65.409 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
entity_1: GSHMSLVTCPICHAPYVEED LLIQCRHCERWMHAGCESLF TEDDVEQAADEGFDCVSCQP YVVK
entity_2: XGKGGAXRHRKVX

Data sets:
Data typeCount
13C chemical shifts219
15N chemical shifts58
1H chemical shifts392

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22
3entity_3, 13
4entity_3, 23

Entities:

Entity 1, entity_1 64 residues - 7240.149 Da.

1   GLYSERHISMETSERLEUVALTHRCYSPRO
2   ILECYSHISALAPROTYRVALGLUGLUASP
3   LEULEUILEGLNCYSARGHISCYSGLUARG
4   TRPMETHISALAGLYCYSGLUSERLEUPHE
5   THRGLUASPASPVALGLUGLNALAALAASP
6   GLUGLYPHEASPCYSVALSERCYSGLNPRO
7   TYRVALVALLYS

Entity 2, entity_2 13 residues - 1264.527 Da.

1   ACEGLYLYSGLYGLYALAALYARGHISARG
2   LYSVALNH2

Entity 3, entity_3, 1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: MLL4 PHD6, [U-13C; U-15N], 2.5 mM; histone H4K16ac (11-21) peptide 7.5 mM; NaCl buffer 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
2D filtered TOCSYsample_1isotropicsample_conditions_1
3D filtered NOESYsample_1isotropicsample_conditions_1
3D NOESY-HSQCsample_1isotropicsample_conditions_1

Software:

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CcpNmr Analysis, CCPN - chemical shift assignment

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

Amber, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, and Kollman - refinement

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 900 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts