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 19521

Title: Solution structure of BCL-xL containing the alpha1-alpha2 disordered loop determined with selective isotope labelling of I,L,V sidechains

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

Citation: Kriwacki, Ariele; Ou, Li; Llambi, Fabien; Green, Douglas; Kriwacki, Richard. "The DNA Binding Domain is a Promiscuous Interaction Hub that Mediates the Nuclear and Cytoplasmic Functions of p53"  Nat. Struct. Biol. ., .-..

Assembly members:
BCL-xL, polymer, 212 residues, 23670.139 Da.

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

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

Entity Sequences (FASTA):
BCL-xL: GHSMSQSNRELVVDFLSYKL SQKGYSWSQFSDVEENRTEA PEGTESEMETPSAINGNPSW HLADSPAVNGATGHSSSLDA REVIPMAAVKQALREAGDEF ELRYRRAFSDLTSQLHITPG TAYQSFEQVVNELFRDGVNW GRIVAFFSFGGALCVESVDK EMQVLVSRIAAWMATYLNDH LEPWIQENGGWDTFVELYGN NAAAESRKGQER

Data sets:
Data typeCount
13C chemical shifts642
15N chemical shifts209
1H chemical shifts1041

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BCL-xL1

Entities:

Entity 1, BCL-xL 212 residues - 23670.139 Da.

The three N terminal residues constitute the leftover of a cleaved 6xHis Tag. The construct bears a deletion of the C terminal 22 residues of the wild type protein for solubility purposes

1   GLYHISSERMETSERGLNSERASNARGGLU
2   LEUVALVALASPPHELEUSERTYRLYSLEU
3   SERGLNLYSGLYTYRSERTRPSERGLNPHE
4   SERASPVALGLUGLUASNARGTHRGLUALA
5   PROGLUGLYTHRGLUSERGLUMETGLUTHR
6   PROSERALAILEASNGLYASNPROSERTRP
7   HISLEUALAASPSERPROALAVALASNGLY
8   ALATHRGLYHISSERSERSERLEUASPALA
9   ARGGLUVALILEPROMETALAALAVALLYS
10   GLNALALEUARGGLUALAGLYASPGLUPHE
11   GLULEUARGTYRARGARGALAPHESERASP
12   LEUTHRSERGLNLEUHISILETHRPROGLY
13   THRALATYRGLNSERPHEGLUGLNVALVAL
14   ASNGLULEUPHEARGASPGLYVALASNTRP
15   GLYARGILEVALALAPHEPHESERPHEGLY
16   GLYALALEUCYSVALGLUSERVALASPLYS
17   GLUMETGLNVALLEUVALSERARGILEALA
18   ALATRPMETALATHRTYRLEUASNASPHIS
19   LEUGLUPROTRPILEGLNGLUASNGLYGLY
20   TRPASPTHRPHEVALGLULEUTYRGLYASN
21   ASNALAALAALAGLUSERARGLYSGLYGLN
22   GLUARG

Samples:

sample_1: BCL-xL, [U- 98% 13C; U- 98% 15N; U- 98% 2H; U- I,LV CH3 1H], 0.6 mM; sodium phosphate 10 mM; sodium chloride 40 mM; DTT 5 mM; NaN3 0.01%; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 0.05 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CARA, Keller, R.L.J. - chemical shift assignment, data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

GB CAA80661 AAA51039 AAA82173 AAA82174 AAB17352 AAB17353
BMRB 19520 19522
PDB
DBJ BAB71819 BAB85856 BAE27189 BAE42906 BAE73044
EMBL CAA04597 CAA57886 CAA58557 CAA80661 CAI56777
REF NP_001003072 NP_001009226 NP_001009228 NP_001028842 NP_001028844
SP O77737 P53563 Q07817 Q64373
TPG DAA23121