BMRB Entry 25087

Name: Resonance assignments of myristoylated Y28F/Y67F mutant of the Mason-Pfizer monkey virus matrix protein
Published: 2015-03-24

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PDB ID: 2mv4
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25087
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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:

Resonance assignments of myristoylated Y28F/Y67F mutant of the Mason-Pfizer monkey virus matrix protein

Deposition date:

2014-07-14

Original release date:

2015-03-24

Authors:

Dolezal, Michal; Hrabal, Richard

Citation:

Citation: Dolezal, Michal; Hrabal, Richard; Ruml, Tomas; Rumlova, Michaela. "Resonance assignments of myristoylated Y28F/Y67F mutant of the Mason-Pfizer monkey virus matrix protein" Biomol. NMR Assignments ., .-. (2015).
PubMed: 25773138

Assembly members:

Assembly members:
MPMV_MA_Y28F_Y67F, polymer, 125 residues, 14867.84 Da.

Natural source:

Natural source: Common Name: Mason-Pfizer monkey virus Taxonomy ID: 11855 Superkingdom: Viruses Kingdom: not available Genus/species: Betaretrovirus Mason-Pfizer monkey virus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MPMV_MA_Y28F_Y67F: XGQELSQHERYVEQLKQALK TRGVKVKFADLLKFFDFVKD TCPWFPQEGTIDIKRWRRVG DCFQDYFNTFGPEKVPVTAF SYWNLIKELIDKKEVNPQVM AAVAQTEEILKSNSQTDLEH HHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list

Data type	Count
1H chemical shifts	913
13C chemical shifts	575
15N chemical shifts	141

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MPMV_MA_Y28F_Y67F	1

Entities:

Entity 1, MPMV_MA_Y28F_Y67F 125 residues - 14867.84 Da.

the protein is N-terminally myristoylated

1

MYR

GLY

GLN

GLU

LEU

SER

GLN

HIS

GLU

ARG

2

TYR

VAL

GLU

GLN

LEU

LYS

GLN

ALA

LEU

LYS

3

THR

ARG

GLY

VAL

LYS

VAL

LYS

PHE

ALA

ASP

4

LEU

LYS

PHE

ASP

PHE

VAL

LYS

ASP

5

THR

CYS

PRO

TRP

PHE

PRO

GLN

GLU

GLY

THR

6

ILE

ASP

ILE

LYS

ARG

TRP

ARG

VAL

GLY

7

ASP

CYS

PHE

GLN

ASP

TYR

PHE

ASN

THR

PHE

8

GLY

PRO

GLU

LYS

VAL

PRO

VAL

THR

ALA

PHE

9

SER

TYR

TRP

ASN

LEU

ILE

LYS

GLU

LEU

ILE

10

ASP

LYS

GLU

VAL

ASN

PRO

GLN

VAL

MET

11

ALA

VAL

ALA

GLN

THR

GLU

ILE

LEU

12

LYS

SER

ASN

SER

GLN

THR

ASP

LEU

GLU

HIS

13

HIS

Samples:

sample_1: MPMV_MA_Y28F_Y67F, [U-99% 13C; U-99% 15N; NA-MYR], 1.0 mM; NaCl 300.0 mM; TCEP 2.5 mM; sodium phosphate 50.0 mM; H2O 95%; D2O 5%

sample_2: MPMV_MA_Y28F_Y67F, [U-99% 13C; U-99% 15N; NA-MYR,H], 1.0 mM; NaCl 300.0 mM; TCEP 2.5 mM; sodium phosphate 50.0 mM; H2O 95%; D2O 5%

sample_3: MPMV_MA_Y28F_Y67F, [U-99% 13C; U-99% 15N], 1.0 mM; NaCl 300.0 mM; TCEP 2.5 mM; sodium phosphate 50.0 mM; H2O 95%; D2O 5%

sample_4: MPMV_MA_Y28F_Y67F, [U-99% 13C]-MYR, 1.0 mM; NaCl 300.0 mM; TCEP 2.5 mM; sodium phosphate 50.0 mM; H2O 95%; D2O 5%

CondSet1: ionic strength: 0.600 M; pH: 6.000; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	CondSet1
2D 1H-13C HSQC	sample_1	isotropic	CondSet1
2D 1H-13C HSQC	sample_3	isotropic	CondSet1
2D 1H-13C HSQC	sample_4	isotropic	CondSet1
2D CON	sample_1	isotropic	CondSet1
2D CaCO	sample_1	isotropic	CondSet1
3D HNCO	sample_1	isotropic	CondSet1
3D HNCO	sample_3	isotropic	CondSet1
3D HNCA	sample_1	isotropic	CondSet1
3D HNCA	sample_3	isotropic	CondSet1
3D CBCA(CO)NH	sample_1	isotropic	CondSet1
3D CBCA(CO)NH	sample_3	isotropic	CondSet1
3D HNCACB	sample_1	isotropic	CondSet1
3D HBHA(CBCACO)NH	sample_1	isotropic	CondSet1
3D H(CCCO)NH-TOCSY	sample_1	isotropic	CondSet1
3D HC(C)H-COSY	sample_4	isotropic	CondSet1
3D HC(C)H-TOCSY	sample_1	isotropic	CondSet1
3D HC(C)H-TOCSY	sample_4	isotropic	CondSet1
3D (H)CCH-COSY	sample_4	isotropic	CondSet1
3D (H)CCH-TOCSY	sample_1	isotropic	CondSet1
3D (H)CCH-TOCSY	sample_4	isotropic	CondSet1
2D 1H-13C HSQC aro	sample_2	isotropic	CondSet1
2D (HB)CB(CGCD)HD	sample_2	isotropic	CondSet1
2D (HB)CB(CGCDCE)HE	sample_2	isotropic	CondSet1
2D (H)CB(CGCC-TOCSY)Har-phe	sample_2	isotropic	CondSet1
2D (H)CB(CGCC-TOCSY)Har-trp	sample_2	isotropic	CondSet1
2D (H)CB(CGCC-TOCSY)Har-tyr	sample_2	isotropic	CondSet1

Software:

CcpNmr_Analysis v2.3, CCPN - resonance assignment

Topspin v3.2, Bruker - spectra procession

NMR spectrometers:

Bruker Avance 600 MHz

BMRB	18282
PDB	1BAX 2F76 2F77 2LPY 2MV4
GB	AAA47710 AAC82573 AAC82574 AAC82576 ABD83648
REF	NP_056891 NP_056892 NP_056893 NP_954557 NP_954565
SP	P07567
AlphaFold	P07567