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 18792

Title: Solution structure of BCL-xL determined with selective isotope labelling of I,L,V sidechains   PubMed: 23340338

Deposition date: 2012-10-19 Original release date: 2013-01-22

Authors: Viacava Follis, Ariele; Royappa, Grace; Kriwacki, Richard

Citation: Follis, Ariele Viacava; Chipuk, Jerry; Fisher, John; Yun, Mi-Kyung; Grace, Christy; Nourse, Amanda; Baran, Katherine; Ou, Li; Min, Lie; White, Stephen; Green, Douglas; Kriwacki, Richard. "PUMA binding induces partial unfolding within BCL-xL to disrupt p53 binding and promote apoptosis."  Nat. Chem. Biol. 9, 163-168 (2013).

Assembly members:
BCL-xL_apo, polymer, 181 residues, 20252.496 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):
BCL-xL_apo: MSMAMSQSNRELVVDFLSYK LSQKGYSWSQFSDVEENRTE APEGTESEAVKQALREAGDE FELRYRRAFSDLTSQLHITP GTAYQSFEQVVNELFRDGVN WGRIVAFFSFGGALCVESVD KEMQVLVSRIAAWMATYLND HLEPWIQENGGWDTFVELYG NNAAAESRKGQERLEHHHHH H

Data sets:
Data typeCount
13C chemical shifts536
15N chemical shifts171
1H chemical shifts343

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BCL-xL_apo1

Entities:

Entity 1, BCL-xL_apo 181 residues - 20252.496 Da.

Wild-type Human protein with truncation of 22 C terminal residues and disordered loop between alpha helices 1 and 2

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_apo, [U-100% 13C; U-100% 15N; U-95% 2H; Ile,Leu,Val C1H3], 0.9 mM; sodium phosphate 10 mM; sodium chloride 40 mM; NaN3 0.1%; H2O 92%; D2O 8%

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

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

CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, peak picking, structure solution

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

GB CAA80661

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