BMRB Entry 18340

Title:
Structural Mechanism for Bax Inhibition by Cytomegalovirus Protein vMIA
Deposition date:
2012-03-20
Original release date:
2012-12-04
Authors:
Ma, Junhe
Citation:

Citation: Ma, Junhe; Edlich, Frank; Bermejo, Guillermo; Norris, Kristi; Youle, Richard; Tjandra, Nico. "Structural mechanism of Bax inhibition by cytomegalovirus protein vMIA."  Proc. Natl. Acad. Sci. U.S.A. 109, 20901-20906 (2012).
PubMed: 23213219

Assembly members:

Assembly members:
entity_1, polymer, 192 residues, 21204.494 Da.
entity_2, polymer, 21 residues, 2732.313 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   Vector: pET28

Data sets:
Data typeCount
13C chemical shifts38
15N chemical shifts11
1H chemical shifts124

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Bax1
2vMIA2

Entities:

Entity 1, Bax 192 residues - 21204.494 Da.

1   METASPGLYSERGLYGLUGLNPROARGGLY
2   GLYGLYPROTHRSERSERGLUGLNILEMET
3   LYSTHRGLYALALEULEULEUGLNGLYPHE
4   ILEGLNASPARGALAGLYARGMETGLYGLY
5   GLUALAPROGLULEUALALEUASPPROVAL
6   PROGLNASPALASERTHRLYSLYSLEUSER
7   GLUCYSLEULYSARGILEGLYASPGLULEU
8   ASPSERASNMETGLULEUGLNARGMETILE
9   ALAALAVALASPTHRASPSERPROARGGLU
10   VALPHEPHEARGVALALAALAASPMETPHE
11   SERASPGLYASNPHEASNTRPGLYARGVAL
12   VALALALEUPHETYRPHEALASERLYSLEU
13   VALLEULYSALALEUCYSTHRLYSVALPRO
14   GLULEUILEARGTHRILEMETGLYTRPTHR
15   LEUASPPHELEUARGGLUARGLEULEUGLY
16   TRPILEGLNASPGLNGLYGLYTRPASPGLY
17   LEULEUSERTYRPHEGLYTHRPROTHRTRP
18   GLNTHRVALTHRILEPHEVALALAGLYVAL
19   LEUTHRALASERLEUTHRILETRPLYSLYS
20   METGLY

Entity 2, vMIA 21 residues - 2732.313 Da.

1   CYSGLUALALEULYSLYSALALEUARGARG
2   HISARGPHELEUTRPGLNARGARGGLNARG
3   ALA

Samples:

sample_2: entity_1 0.1 mM; entity_2, [U-100% 13C; U-100% 15N], 0.1 mM; potassium phosphate 20 mM; D2O, [U-100% 2H], 10%; H2O 90%; DTT 0 mM

sample_1: entity_1, [U-100% 15N], 0.1 mM; entity_2 0.1 mM; potassium phosphate 20 mM; D2O, [U-100% 2H], 10%; H2O 90%; DTT 0 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6.2; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D DQF-COSYsample_2isotropicsample_conditions_1

Software:

X-PLOR, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

BMRB 4632
PDB
DBJ BAC53619 BAF83765 BAI46883
EMBL CAD10744 CCF78739 CAA35396
GB AAA03619 AAA03620 AAC48806 AAD22706 AAF82094 AAK01675 AAK01676 AAK01677 AAK01678 AAK01679
REF NP_001003011 NP_001247945 NP_001278357 NP_001278358 NP_001278360 YP_081496
SP O02703 Q07812 P16778 Q6SW94
TPG DAA19512 DAA00142
AlphaFold O02703 Q07812 Q6SW94 P16778

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