BMRB Entry 25087

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

Data sets:
Data typeCount
1H chemical shifts913
13C chemical shifts575
15N chemical shifts141

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MPMV_MA_Y28F_Y67F1

Entities:

Entity 1, MPMV_MA_Y28F_Y67F 125 residues - 14867.84 Da.

the protein is N-terminally myristoylated

1   MYRGLYGLNGLULEUSERGLNHISGLUARG
2   TYRVALGLUGLNLEULYSGLNALALEULYS
3   THRARGGLYVALLYSVALLYSPHEALAASP
4   LEULEULYSPHEPHEASPPHEVALLYSASP
5   THRCYSPROTRPPHEPROGLNGLUGLYTHR
6   ILEASPILELYSARGTRPARGARGVALGLY
7   ASPCYSPHEGLNASPTYRPHEASNTHRPHE
8   GLYPROGLULYSVALPROVALTHRALAPHE
9   SERTYRTRPASNLEUILELYSGLULEUILE
10   ASPLYSLYSGLUVALASNPROGLNVALMET
11   ALAALAVALALAGLNTHRGLUGLUILELEU
12   LYSSERASNSERGLNTHRASPLEUGLUHIS
13   HISHISHISHISHIS

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicCondSet1
2D 1H-13C HSQCsample_1isotropicCondSet1
2D 1H-13C HSQCsample_3isotropicCondSet1
2D 1H-13C HSQCsample_4isotropicCondSet1
2D CONsample_1isotropicCondSet1
2D CaCOsample_1isotropicCondSet1
3D HNCOsample_1isotropicCondSet1
3D HNCOsample_3isotropicCondSet1
3D HNCAsample_1isotropicCondSet1
3D HNCAsample_3isotropicCondSet1
3D CBCA(CO)NHsample_1isotropicCondSet1
3D CBCA(CO)NHsample_3isotropicCondSet1
3D HNCACBsample_1isotropicCondSet1
3D HBHA(CBCACO)NHsample_1isotropicCondSet1
3D H(CCCO)NH-TOCSYsample_1isotropicCondSet1
3D HC(C)H-COSYsample_4isotropicCondSet1
3D HC(C)H-TOCSYsample_1isotropicCondSet1
3D HC(C)H-TOCSYsample_4isotropicCondSet1
3D (H)CCH-COSYsample_4isotropicCondSet1
3D (H)CCH-TOCSYsample_1isotropicCondSet1
3D (H)CCH-TOCSYsample_4isotropicCondSet1
2D 1H-13C HSQC arosample_2isotropicCondSet1
2D (HB)CB(CGCD)HDsample_2isotropicCondSet1
2D (HB)CB(CGCDCE)HEsample_2isotropicCondSet1
2D (H)CB(CGCC-TOCSY)Har-phesample_2isotropicCondSet1
2D (H)CB(CGCC-TOCSY)Har-trpsample_2isotropicCondSet1
2D (H)CB(CGCC-TOCSY)Har-tyrsample_2isotropicCondSet1

Software:

CcpNmr_Analysis v2.3, CCPN - resonance assignment

Topspin v3.2, Bruker - spectra procession

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 18282
PDB
GB AAA47710 AAC82573 AAC82574 AAC82576 ABD83648
REF NP_056891 NP_056892 NP_056893 NP_954557 NP_954565
SP P07567
AlphaFold P07567

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