BMRB Entry 34603

Title:
Solution structure of MLKL executioner domain in complex with a fragment
Deposition date:
2021-02-23
Original release date:
2021-09-17
Authors:
Ruebbelke, M.; Bauer, M.; Hamilton, J.; Binder, F.; Nar, H.; Zeeb, M.
Citation:

Citation: Ruebbelke, M.; Hamilton, J.; Binder, F.; Bauer, M.; King, J.; Nar, H.; Zeeb, M.. "Discovery and Structure-Based Optimization of Fragments Binding the Mixed Lineage Kinase Domain-like Protein Executioner Domain"  J. Med. Chem. 64, 15629-15638 (2021).
PubMed: 34672548

Assembly members:

Assembly members:
entity_1, polymer, 157 residues, 18184.961 Da.
entity_UJ5, non-polymer, 324.374 Da.

Natural source:

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

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts510
15N chemical shifts158
1H chemical shifts1062

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_22

Entities:

Entity 1, unit_1 157 residues - 18184.961 Da.

1   GLYSERPROGLYGLUASNLEULYSHISILE
2   ILETHRLEUGLYGLNVALILEHISLYSARG
3   CYSGLUGLUMETLYSTYRCYSLYSLYSGLN
4   CYSARGARGLEUGLYHISARGVALLEUGLY
5   LEUILELYSPROLEUGLUMETLEUGLNASP
6   GLNGLYLYSARGSERVALPROSERGLULYS
7   LEUTHRTHRALAMETASNARGPHELYSALA
8   ALALEUGLUGLUALAASNGLYGLUILEGLU
9   LYSPHESERASNARGSERASNILECYSARG
10   PHELEUTHRALASERGLNASPLYSILELEU
11   PHELYSASPVALASNARGLYSLEUSERASP
12   VALTRPLYSGLULEUSERLEULEULEUGLN
13   VALGLUGLNARGMETPROVALSERPROILE
14   SERGLNGLYALASERTRPALAGLNGLUASP
15   GLNGLNASPALAASPGLUASPARGARGALA
16   PHEGLNMETLEUARGARGASP

Entity 2, unit_2 - C19 H20 N2 O3 - 324.374 Da.

1   UJ5

Samples:

sample_1: MLKL executioner domain, [U-13C; U-15N], 430 uM; Cpd 5 700 uM

sample_2: MLKL executioner domain, [U-13C; U-15N], 400 uM; Cpd 5 700 uM

sample_conditions_1: ionic strength: 170 mM; pH: 7.1; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 170 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
3D HNCACBsample_2isotropicsample_conditions_2
3D HNccH TOCSYsample_2isotropicsample_conditions_2
3D HNCC TOCSYsample_2isotropicsample_conditions_2
3D 1H-15N NOESYsample_2isotropicsample_conditions_2
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D filt. 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1

Software:

CYANA v3.98.9, Guntert, Mumenthaler and Wuthrich - structure calculation

CcpNmr Analysis v2.4.2, CCPN - chemical shift assignment, peak picking

TopSpin v3.5, Bruker Biospin - processing

TopSpin v3.6, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks