BMRB Entry 34029

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34029
MolProbity Validation Chart

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Title:
Solution structure of the m-pmv myristoylated matrix protein
Deposition date:
2016-08-02
Original release date:
2016-09-30
Authors:
Prchal, J.; Hrabal, R.
Citation:

Citation: Prchal, J.; Srb, P.; Hunter, E.; Ruml, T.; Hrabal, R.. "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).
PubMed: 22863803

Assembly members:

Assembly members:
entity_1, polymer, 125 residues, 14923.988 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: XGQELSQHERYVEQLKQALK TRGVKVKYADLLKFFDFVKD TCPWFPQEGTIDIKRWRRVG DCFQDYYNTFGPEKVPVTAF SYWNLIKELIDKKEVNPQVM AAVAQTEEILKSNSQTDLEH HHHHH

Data sets:
Data typeCount
13C chemical shifts420
15N chemical shifts116
1H chemical shifts533

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 125 residues - 14923.988 Da.

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

Samples:

sample_1: DTT 5 mM; Matrix protein p10, [U-99% 13C; U-99% 15N], 1.2 mM; potassium phosphate 100 mM; sodium chloride 300 mM

sample_2: DTT 5 mM; Matrix protein p10, [U-99% 15N], 0.2 mM; Pf1 phage 10 mg/mL; potassium phosphate 50 mM; sodium chloride 150 mM

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

sample_conditions_2: ionic strength: 300 mM; 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 CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQC IPAPsample_2anisotropicsample_conditions_2

Software:

Analysis v2.1.5, CCPN - chemical shift assignment

TALOS+, Cornilescu, Delaglio and Bax - geometry optimization

TOPSPIN v3.5, Bruker Biospin - collection

X-PLOR NIH v2.24, 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