BMRB Entry 26580

Name: Structure of herpesvirus nuclear egress complex subunit M50
Published: 2015-07-13

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PDB ID: 5a3g
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26580
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Structure of herpesvirus nuclear egress complex subunit M50

Deposition date:

2015-06-01

Original release date:

2015-07-13

Authors:

Leigh, Kendra; Boeszoermenyi, Andras; Mansueto, My; Sharma, Mayuri; Filman, David; Coen, Donald; Wagner, Gerhard; Hogle, James; Arthanari, Haribabu

Citation:

Citation: Leigh, Kendra; Sharma, Mayuri; Mansueto, My Sam; Boeszoermenyi, Andras; Filman, David; Hogle, James; Wagner, Gerhard; Coen, Donald; Arthanari, Haribabu. "Structure of a herpesvirus nuclear egress complex subunit reveals an interaction groove that is essential for viral replication" Proc. Natl. Acad. Sci. U. S. A. 112, 9010-9015 (2015).
PubMed: 26150520

Assembly members:

Assembly members:
M50, polymer, 171 residues, 19379.2143 Da.

Natural source:

Natural source: Common Name: Murine cytomegalovirus Taxonomy ID: 10366 Superkingdom: Viruses Kingdom: not available Genus/species: Murine cytomegalovirus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: IMPACT-CN pTYB12

Entity Sequences (FASTA):

Entity Sequences (FASTA):
M50: AGHMEIDKNVGADLISNTRR ILRLDENELRITDTALICKN PNYSLCDAMLTTDIVYPVEY LLSYWECRSGRTACFVFKNT GCRVSLSCYIGFPERLKDLK RVCDFNFLSVNEALVVTLAD IERIKPCDKGVLTNCVVRKS NSGMSYNIEVVAFGPDNEAE YQALLRDIYAR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_1_2

Data type	Count
13C chemical shifts	707
15N chemical shifts	162
1H chemical shifts	1205

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	M50	1

Entities:

Entity 1, M50 171 residues - 19379.2143 Da.

1

ALA

GLY

HIS

MET

GLU

ILE

ASP

LYS

ASN

VAL

2

GLY

ALA

ASP

LEU

ILE

SER

ASN

THR

ARG

3

ILE

LEU

ARG

LEU

ASP

GLU

ASN

GLU

LEU

ARG

4

ILE

THR

ASP

THR

ALA

LEU

ILE

CYS

LYS

ASN

5

PRO

ASN

TYR

SER

LEU

CYS

ASP

ALA

MET

LEU

6

THR

ASP

ILE

VAL

TYR

PRO

VAL

GLU

TYR

7

LEU

SER

TYR

TRP

GLU

CYS

ARG

SER

GLY

8

ARG

THR

ALA

CYS

PHE

VAL

PHE

LYS

ASN

THR

9

GLY

CYS

ARG

VAL

SER

LEU

SER

CYS

TYR

ILE

10

GLY

PHE

PRO

GLU

ARG

LEU

LYS

ASP

LEU

LYS

11

ARG

VAL

CYS

ASP

PHE

ASN

PHE

LEU

SER

VAL

12

ASN

GLU

ALA

LEU

VAL

THR

LEU

ALA

ASP

13

ILE

GLU

ARG

ILE

LYS

PRO

CYS

ASP

LYS

GLY

14

VAL

LEU

THR

ASN

CYS

VAL

ARG

LYS

SER

15

ASN

SER

GLY

MET

SER

TYR

ASN

ILE

GLU

VAL

16

VAL

ALA

PHE

GLY

PRO

ASP

ASN

GLU

ALA

GLU

17

TYR

GLN

ALA

LEU

ARG

ASP

ILE

TYR

ALA

18

ARG

Samples:

M50_TL: M50, [U-13C; U-15N], 0.23 mM; NaPO4 25 mM; NaCl 150 mM; DTT 1 mM

M50_DL: M50, [U-13C; U-15N], 0.23 mM; NaPO4 25 mM; NaCl 150 mM; DTT 1 mM

M50_DL_60%deut: M50, [U-13C; U-15N], 0.23 mM; NaPO4 25 mM; NaCl 150 mM; DTT 1 mM

M50_ILV: M50, [U-13C; U-15N], 0.23 mM; NaPO4 25 mM; NaCl 150 mM; DTT 1 mM

sample_new_1: M50, [U-13C; U-15N], 230 uM; NaPO4 25 mM; NaCl 150 mM; DTT 1 mM

1: ionic strength: 175.000 mM; pH: 6.500; pressure: 1.000 atm; temperature: 291.150 K

2: ionic strength: 175.000 mM; pH: 6.500; pressure: 1.000 atm; temperature: 291.150 K

3: ionic strength: 175.000 mM; pH: 6.500; pressure: 1.000 atm; temperature: 291.150 K

Experiments:

Name	Sample	Sample state	Sample conditions
15N_TROSY	M50_TL	isotropic	1
TROSY_HNCA	M50_TL	isotropic	1
TROSY_HNCACB	M50_TL	isotropic	1
15NNOESYhsqc	M50_DL	isotropic	1
TROSY_HNCACO	M50_TL	isotropic	1
HCCONH	M50_DL_60%deut	isotropic	1
CCONH	M50_DL_60%deut	isotropic	1
HCCH-TOCSY	M50_DL_60%deut	isotropic	1
13CHSQC	M50_DL	isotropic	2
13NOESYhsqc	M50_DL	isotropic	2
15N_ILV_NOESY	M50_ILV	isotropic	1
13C_ILV_NOESY	M50_ILV	isotropic	1
4D 13CHMQC-NOESY-HMQC	M50_ILV	isotropic	2
RDC_HNCO	M50_TL	anisotropic	3
TROSY_HNCO	M50_TL	isotropic	1
TROSY_HNCOCA	M50_TL	isotropic	1
13C_ILV_HSQC	M50_ILV	isotropic	2
15N TROSY	sample_new_1	solution	1
TROSY HNCA	sample_new_1	solution	1
TROSY HNCACB	sample_new_1	solution	1
TROSY HNCACO	sample_new_1	solution	1

Software:

AMBER vWeNMR-GRID, AMPS-NMR - RDC and Waterbox Refinement

CARA v1.8.4, N. Schaefer - Resonance Assignment and Peak Picking

CYANA v3.0, Guntert, Mumentaler, and Wuthrich - Simulated Annealing

CcpNmr_Analysis v2.4, CCPN - 4D Analysis

TALOS+ v1.2009.0605.17, Shen, Cornilescu, Delaglio, and Bax - Generation of Dihedral Angle Restraints

hmsIST v2.11, S. Hyberts - Processing of Non Uniformly Sampled Spectra

nmrDraw v11, F. Delaglio - Spectrum Display

nmrPipe v11, F. Delaglio - Spectrum Processing

NMR spectrometers:

Bruker Avance 750 MHz
Bruker Avance 900 MHz
Bruker Avance 600 MHz
Varian dd2 600 MHz
Bruker AVANCE 750 MHz
Varian UNITYINOVA 600 MHz

UNP	H2A365_MUHV1
AlphaFold	H2A365