BMRB Entry 34015

Name: Myristoylated T41I/T78I mutant of M-PMV matrix protein
Published: 2016-07-21

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PDB ID: 5ldl
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34015
MolProbity Validation Chart

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

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Title:

Myristoylated T41I/T78I mutant of M-PMV matrix protein

Deposition date:

2016-06-27

Original release date:

2016-07-21

Authors:

Kroupa, T.; Hrabal, R.

Citation:

Citation: Kroupa, Tomas; Langerova, Hana; Dolezal, Michal; Prchal, Jan; Spiwok, Vojtech; Hunter, Eric; Rumlova, Michaela; Hrabal, Richard; Ruml, Tomas. "Membrane interaction of the Mason-Pfizer monkey virus matrix protein and its budding deficient mutants" J. Mol. Biol. 428, 4708-4722 (2016).
PubMed: 27725181

Assembly members:

Assembly members:
entity_1, polymer, 124 residues, 14737.740 Da.
entity_MYR, non-polymer, 228.371 Da.

Natural source:

Natural source: Common Name: MPMV Taxonomy ID: 11855 Superkingdom: Viruses Kingdom: not available Genus/species: Betaretrovirus MPMV

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GQELSQHERYVEQLKQALKT RGVKVKYADLLKFFDFVKDI CPWFPQEGTIDIKRWRRVGD CFQDYYNTFGPEKVPVIAFS YWNLIKELIDKKEVNPQVMA AVAQTEEILKSNSQTDLEHH HHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	374
15N chemical shifts	100
1H chemical shifts	687

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_MYR	2

Entities:

Entity 1, entity_1 124 residues - 14737.740 Da.

1

GLY

GLN

GLU

LEU

SER

GLN

HIS

GLU

ARG

TYR

2

VAL

GLU

GLN

LEU

LYS

GLN

ALA

LEU

LYS

THR

3

ARG

GLY

VAL

LYS

VAL

LYS

TYR

ALA

ASP

LEU

4

LEU

LYS

PHE

ASP

PHE

VAL

LYS

ASP

ILE

5

CYS

PRO

TRP

PHE

PRO

GLN

GLU

GLY

THR

ILE

6

ASP

ILE

LYS

ARG

TRP

ARG

VAL

GLY

ASP

7

CYS

PHE

GLN

ASP

TYR

ASN

THR

PHE

GLY

8

PRO

GLU

LYS

VAL

PRO

VAL

ILE

ALA

PHE

SER

9

TYR

TRP

ASN

LEU

ILE

LYS

GLU

LEU

ILE

ASP

10

LYS

GLU

VAL

ASN

PRO

GLN

VAL

MET

ALA

11

ALA

VAL

ALA

GLN

THR

GLU

ILE

LEU

LYS

12

SER

ASN

SER

GLN

THR

ASP

LEU

GLU

HIS

13

HIS

Entity 2, entity_MYR - C14 H28 O2 - 228.371 Da.

1

MYR

Samples:

sample_1: DTT, none, 5 mM; myristoylated retroviral matrix protein, [U-13C; U-15N], 1 mM; phosphate, none, 100 mM; sodium choride, none, 300 mM

sample_2: DTT, none, 5 mM; Pf1 phage, none, 10 mg/mL; myristoylated retroviral matrix protein, [U-15N], 400 mM; phosphate, none, 50 mM; sodium choride, none, 150 mM

sample_conditions_1: ionic strength: 600 mM; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC IPAP	sample_2	anisotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR, CCPN - peak picking

TOPSPIN, Bruker Biospin - collection, processing

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

NMR spectrometers:

Bruker AvanceIII 600 MHz

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