BMRB Entry 30610

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30610
MolProbity Validation Chart

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Title:
hMcl1 inhibitor complex
Deposition date:
2019-05-07
Original release date:
2019-05-17
Authors:
Poppe, L.
Citation:

Citation: Caenepeel, S.; Brown, S.; Belmontes, B.; Moody, G.; Keegan, K.; Chui, D.; Whittington, D.; Huang, X.; Poppe, L.; Cheng, A.; Cardozo, M.; Houze, J.; Li, Y.; Lucas, B.; Paras, N.; Wang, X.; Taygerly, J.; Vimolratana, M.; Zancanella, M.; Zhu, L.; Cajulis, E.; Osgood, T.; Sun, J.; Damon, L.; Egan, R.; Greninger, P.; McClanaghan, J.; Gong, J.; Moujalled, D.; Pomilio, G.; Beltran, P.; Benes, C.; Roberts, A.; Huang, D.; Wei, A.; Canon, J.; Coxon, A.; Hughes, P.. "AMG 176, a Selective MCL1 Inhibitor, Is Effective in Hematologic Cancer Models Alone and in Combination with Established Therapies."  Cancer Discov. 8, 1582-1597 (2018).
PubMed: 30254093

Assembly members:

Assembly members:
entity_1, polymer, 164 residues, 18866.354 Da.
entity_N8J, non-polymer, 545.477 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 K-12

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MEDELYRQSLEIISRYLREQ ATGAKDTKPMGRSGATSRKA LETLRRVGDGVQRNHETAFQ GMLRKLDIKNEDDVKSLSRV MIHVFSDGVTNWGRIVTLIS FGAFVAKHLKTINQESSIEP LAESITDVLVRTKRDWLVKQ RGWDGFVEFFHVEDLEGGHH HHHH

Data sets:
Data typeCount
13C chemical shifts548
15N chemical shifts175
1H chemical shifts1153

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 164 residues - 18866.354 Da.

1   METGLUASPGLULEUTYRARGGLNSERLEU
2   GLUILEILESERARGTYRLEUARGGLUGLN
3   ALATHRGLYALALYSASPTHRLYSPROMET
4   GLYARGSERGLYALATHRSERARGLYSALA
5   LEUGLUTHRLEUARGARGVALGLYASPGLY
6   VALGLNARGASNHISGLUTHRALAPHEGLN
7   GLYMETLEUARGLYSLEUASPILELYSASN
8   GLUASPASPVALLYSSERLEUSERARGVAL
9   METILEHISVALPHESERASPGLYVALTHR
10   ASNTRPGLYARGILEVALTHRLEUILESER
11   PHEGLYALAPHEVALALALYSHISLEULYS
12   THRILEASNGLNGLUSERSERILEGLUPRO
13   LEUALAGLUSERILETHRASPVALLEUVAL
14   ARGTHRLYSARGASPTRPLEUVALLYSGLN
15   ARGGLYTRPASPGLYPHEVALGLUPHEPHE
16   HISVALGLUASPLEUGLUGLYGLYHISHIS
17   HISHISHISHIS

Entity 2, entity_2 - C27 H26 Cl2 N2 O4 S - 545.477 Da.

1   N8J

Samples:

sample_1: human Mcl1 protein, [U-99% 13C; U-99% 15N], 0.5 mM; small molecule 0.5 mM; sodium phosphate 20 mM; sodium chloride 50 mM

sample_2: small molecule 0.25 mg/L; hMcl1 protein, [U-99% 13C; U-99% 15N], 0.5 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 50 mM; pH: 7.4; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D X-filtered NOESYsample_1isotropicsample_conditions_1
2D X filtered NOESY-HSQCsample_1isotropicsample_conditions_1
2D HSQC-NOESYsample_2isotropicsample_conditions_2

Software:

TopSpin v3.0, Bruker Biospin - data analysis

Matlab, MathWorks, Inc. - structure calculation

MOE, CCG - refinement

NMR spectrometers:

  • Bruker Avance 800 MHz

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