BMRB Entry 18340

Name: Structural Mechanism for Bax Inhibition by Cytomegalovirus Protein vMIA
Published: 2012-12-04

Click here to enlarge.

PDB ID: 2lr1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18340
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MDGSGEQPRGGGPTSSEQIM KTGALLLQGFIQDRAGRMGG EAPELALDPVPQDASTKKLS ECLKRIGDELDSNMELQRMI AAVDTDSPREVFFRVAADMF SDGNFNWGRVVALFYFASKL VLKALCTKVPELIRTIMGWT LDFLRERLLGWIQDQGGWDG LLSYFGTPTWQTVTIFVAGV LTASLTIWKKMG
entity_2: CEALKKALRRHRFLWQRRQR A

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	38
15N chemical shifts	11
1H chemical shifts	124

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Bax	1
2	vMIA	2

Entities:

Entity 1, Bax 192 residues - 21204.494 Da.

1

MET

ASP

GLY

SER

GLY

GLU

GLN

PRO

ARG

GLY

2

GLY

PRO

THR

SER

GLU

GLN

ILE

MET

3

LYS

THR

GLY

ALA

LEU

GLN

GLY

PHE

4

ILE

GLN

ASP

ARG

ALA

GLY

ARG

MET

GLY

5

GLU

ALA

PRO

GLU

LEU

ALA

LEU

ASP

PRO

VAL

6

PRO

GLN

ASP

ALA

SER

THR

LYS

LEU

SER

7

GLU

CYS

LEU

LYS

ARG

ILE

GLY

ASP

GLU

LEU

8

ASP

SER

ASN

MET

GLU

LEU

GLN

ARG

MET

ILE

9

ALA

VAL

ASP

THR

ASP

SER

PRO

ARG

GLU

10

VAL

PHE

ARG

VAL

ALA

ASP

MET

PHE

11

SER

ASP

GLY

ASN

PHE

ASN

TRP

GLY

ARG

VAL

12

VAL

ALA

LEU

PHE

TYR

PHE

ALA

SER

LYS

LEU

13

VAL

LEU

LYS

ALA

LEU

CYS

THR

LYS

VAL

PRO

14

GLU

LEU

ILE

ARG

THR

ILE

MET

GLY

TRP

THR

15

LEU

ASP

PHE

LEU

ARG

GLU

ARG

LEU

GLY

16

TRP

ILE

GLN

ASP

GLN

GLY

TRP

ASP

GLY

17

LEU

SER

TYR

PHE

GLY

THR

PRO

THR

TRP

18

GLN

THR

VAL

THR

ILE

PHE

VAL

ALA

GLY

VAL

19

LEU

THR

ALA

SER

LEU

THR

ILE

TRP

LYS

20

MET

GLY

Entity 2, vMIA 21 residues - 2732.313 Da.

1

CYS

GLU

ALA

LEU

LYS

ALA

LEU

ARG

2

HIS

ARG

PHE

LEU

TRP

GLN

ARG

GLN

ARG

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
2D DQF-COSY	sample_2	isotropic	sample_conditions_1

Software:

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

NMR spectrometers:

Bruker Avance 800 MHz

BMRB	4632
PDB	1F16 2K7W 2LR1 4BD2 4BD6 4BD7 4BD8 4ZIE 4ZIF 4ZIG 4ZIH 4ZII 2LR1
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 P16778 Q6SW94