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BMRB Entry 18282

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18282
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Title: SOLUTION STRUCTURE OF THE M-PMV MYRISTOYLATED MATRIX PROTEIN   PubMed: 22863803

Deposition date: 2012-02-20 Original release date: 2012-08-21

Authors: Prchal, Jan; Hrabal, Richard

Citation: Prchal, Jan; Srb, Pavel; Hunter, Eric; Ruml, Toma; Hrabal, Richard. "The structure of myristoylated Mason-Pfizer monkey virus matrix protein and the role of phosphatidylinositol-(4,5)-bisphosphate in its membrane binding."  J. Mol. Biol. 423, 427-438 (2012).

Assembly members:
M-PMV_MATRIX_PROTEIN, polymer, 124 residues, 14713.779 Da.
MYR, non-polymer, 228.371 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
M-PMV_MATRIX_PROTEIN: GQELSQHERYVEQLKQALKT RGVKVKYADLLKFFDFVKDT CPWFPQEGTIDIKRWRRVGD CFQDYYNTFGPEKVPVTAFS YWNLIKELIDKKEVNPQVMA AVAQTEEILKSNSQTDLEHH HHHH

Data sets:
Data typeCount
13C chemical shifts419
15N chemical shifts103
1H chemical shifts525

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1M-PMV MYRISTOYLATED MATRIX PROTEIN1
2MYRISTIC ACID2

Entities:

Entity 1, M-PMV MYRISTOYLATED MATRIX PROTEIN 124 residues - 14713.779 Da.

1   GLYGLNGLULEUSERGLNHISGLUARGTYR
2   VALGLUGLNLEULYSGLNALALEULYSTHR
3   ARGGLYVALLYSVALLYSTYRALAASPLEU
4   LEULYSPHEPHEASPPHEVALLYSASPTHR
5   CYSPROTRPPHEPROGLNGLUGLYTHRILE
6   ASPILELYSARGTRPARGARGVALGLYASP
7   CYSPHEGLNASPTYRTYRASNTHRPHEGLY
8   PROGLULYSVALPROVALTHRALAPHESER
9   TYRTRPASNLEUILELYSGLULEUILEASP
10   LYSLYSGLUVALASNPROGLNVALMETALA
11   ALAVALALAGLNTHRGLUGLUILELEULYS
12   SERASNSERGLNTHRASPLEUGLUHISHIS
13   HISHISHISHIS

Entity 2, MYRISTIC ACID - C14 H28 O2 - 228.371 Da.

1   MYR

Samples:

sample_1: potassium phosphate 100 mM; sodium chloride 300 mM; DTT 5 mM; M-PMV MATRIX PROTEIN, [U-99% 13C; U-99% 15N], 0.5 mM; H2O 90%; D2) 10%

sample_conditions_1: ionic strength: 0.4 M; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH v2.24, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

TOPSPIN v2.3, Bruker Biospin - collection

ANALYSIS, Boucher W., Stevens T. - chemical shift assignment, data analysis, peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 25087
PDB
GB AAA47710 AAC82573 AAC82574 AAC82576 ABD83648
REF NP_056891 NP_056892 NP_056893 NP_954557 NP_954565
SP P07567

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