BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 36133

Title: Solution structure of BCL-XL bound to P73-TAD peptide   PubMed: 30429221

Deposition date: 2018-10-11 Original release date: 2018-12-13

Authors: Yoon, M.-K.; Ha, J.-H.; Lee, M.-S.; Chi, S.-W.

Citation: Yoon, M.-K., M.; Kim, B.-Y., B.; Lee, J.-Y., J.; Ha, J.-H., J.; Kim, S.; Lee, D.-H., D.; Lee, M.-S., M.; Lee, M.-K., M.; Choi, J.; Cho, J.; Kim, J.-H., J.; Kim, S.; Song, J.; Park, S.; Park, B.; Bae, K.-H., K.; Choi, S.; Chi, S.-W., S.. "Cytoplasmic pro-apoptotic function of the tumor suppressor p73 is mediated through a modified mode of recognition of the anti-apoptotic regulator Bcl-XL."  J. Biol. Chem. 293, 19546-19558 (2018).

Assembly members:
entity_1, polymer, 16 residues, 1791.846 Da.
entity_2, polymer, 181 residues, 20804.918 Da.

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

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
entity_1: DGGTTFEHLWSSLEPD
entity_2: MSMAMSQSNRELVVDFLSYK LSQKGYSWSQFSDVEENRTE APEGTESEAVKQALREAGDE FELRYRRAFSDLTSQLHITP GTAYQSFEQVVNELFRDGVN WGRIVAFFSFGGALCVESVD KEMQVLVSRIAAWMATYLND HLEPWIQENGGWDTFVELYG NNAAAESRKGQERLEHHHHH H

Data sets:
Data typeCount
13C chemical shifts394
15N chemical shifts164
1H chemical shifts973

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 16 residues - 1791.846 Da.

1   ASPGLYGLYTHRTHRPHEGLUHISLEUTRP
2   SERSERLEUGLUPROASP

Entity 2, entity_2 181 residues - 20804.918 Da.

1   METSERMETALAMETSERGLNSERASNARG
2   GLULEUVALVALASPPHELEUSERTYRLYS
3   LEUSERGLNLYSGLYTYRSERTRPSERGLN
4   PHESERASPVALGLUGLUASNARGTHRGLU
5   ALAPROGLUGLYTHRGLUSERGLUALAVAL
6   LYSGLNALALEUARGGLUALAGLYASPGLU
7   PHEGLULEUARGTYRARGARGALAPHESER
8   ASPLEUTHRSERGLNLEUHISILETHRPRO
9   GLYTHRALATYRGLNSERPHEGLUGLNVAL
10   VALASNGLULEUPHEARGASPGLYVALASN
11   TRPGLYARGILEVALALAPHEPHESERPHE
12   GLYGLYALALEUCYSVALGLUSERVALASP
13   LYSGLUMETGLNVALLEUVALSERARGILE
14   ALAALATRPMETALATHRTYRLEUASNASP
15   HISLEUGLUPROTRPILEGLNGLUASNGLY
16   GLYTRPASPTHRPHEVALGLULEUTYRGLY
17   ASNASNALAALAALAGLUSERARGLYSGLY
18   GLNGLUARGLEUGLUHISHISHISHISHIS
19   HIS

Samples:

sample_1: Bcl-XL, [U-13C; U-15N], 1 mM; p73 peptide 2 mM; H2O 90%; D2O, [U-2H], 10%

sample_2: p73 peptide 1 mM; Bcl-XL 0.1 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 13C/15N-edited NOESY-HSQCsample_1isotropicsample_conditions_1
2D transferred NOESYsample_2isotropicsample_conditions_1
15N/13C-edited, 15N/13C-filtered 3D NOESYsample_1isotropicsample_conditions_1

Software:

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

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AvanceII 800 MHz

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