BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 30738

Title: Solution NMR structure of the myristoylated feline immunodeficiency virus matrix protein

Deposition date: 2020-03-24 Original release date: 2020-07-20

Authors: Brown, J.; Summers, H.; Brown, L.; Marchant, J.; Canova, P.; O'Hern, C.; Abbott, S.; Nyaunu, C.; Maxwell, S.; Johnson, T.; Moser, M.; Ablan, S.; Carter, H.; Freed, E.; Summers, M.

Citation: Brown, J.; Summers, H.; Brown, L.; Marchant, J.; Canova, P.; O'Hern, C.; Abbott, S.; Nyaunu, C.; Maxwell, S.; Johnson, T.; Moser, M.; Ablan, S.; Carter, H.; Freed, E.; Summers, M.. "Solution NMR structure of the myristoylated feline immunodeficiency virus matrix protein"  . ., .-..

Assembly members:
entity_1, polymer, 125 residues, 13922.065 Da.
entity_MYR, non-polymer, 228.371 Da.

Natural source:   Common Name: FIV   Taxonomy ID: 11673   Superkingdom: Viruses   Kingdom: not available   Genus/species: Lentivirus FIV

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

Entity Sequences (FASTA):
entity_1: XGNGQGRDWKMAIKRCSNVA VGVGGKSKKFGEGNFRWAIR MANVSTGREPGDIPETLDQL RLVICDLQERREKFGSSKEI DMAIVTLKVFAVAGLLNMTV STAAAAENMYSQMGLDTRPH HHHHH

Data sets:
Data typeCount
13C chemical shifts449
15N chemical shifts114
1H chemical shifts602

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 125 residues - 13922.065 Da.

1   MYRGLYASNGLYGLNGLYARGASPTRPLYS
2   METALAILELYSARGCYSSERASNVALALA
3   VALGLYVALGLYGLYLYSSERLYSLYSPHE
4   GLYGLUGLYASNPHEARGTRPALAILEARG
5   METALAASNVALSERTHRGLYARGGLUPRO
6   GLYASPILEPROGLUTHRLEUASPGLNLEU
7   ARGLEUVALILECYSASPLEUGLNGLUARG
8   ARGGLULYSPHEGLYSERSERLYSGLUILE
9   ASPMETALAILEVALTHRLEULYSVALPHE
10   ALAVALALAGLYLEULEUASNMETTHRVAL
11   SERTHRALAALAALAALAGLUASNMETTYR
12   SERGLNMETGLYLEUASPTHRARGPROHIS
13   HISHISHISHISHIS

Entity 2, entity_2 - C14 H28 O2 - 228.371 Da.

1   MYR

Samples:

sample_1: sodium phosphate 50 mM; DTT 10 mM; sodium chloride 5 mM; glucose 4 g/L; ammonium chloride, [U-99% 15N], 1 g/L; Feline Immunodeficiency Virus Myristoylated Matrix Protein, [U-15N], 300 uM

sample_2: sodium phosphate 50 mM; DTT, [U-98% 2H], 10 mM; sodium chloride 5 mM; glucose, [U-99% 13C], 4 g/L; ammonium chloride 1 g/L; Feline Immunodeficiency Virus Myristoylated Matrix Protein, [U-13C], 300 uM

sample_3: sodium phosphate 50 mM; DTT, [U-98% 2H], 10 mM; sodium chloride 5 mM; glucose, [U-99% 13C], 4 g/L; ammonium chloride 1 g/L; Feline Immunodeficiency Virus Myristoylated Matrix Protein, [U-13C], 300 uM; Myristoyl coenzyme A 50 mg/L

sample_4: sodium phosphate 50 mM; DTT 10 mM; sodium chloride 5 mM; glucose, [U-99% 13C], 4 g/L; ammonium chloride, [U-99% 15N], 1 g/L; Feline Immunodeficiency Virus Myristoylated Matrix Protein, [U-13C; U-15N], 300 uM

sample_5: sodium phosphate 50 mM; DTT, [U-98% 2H], 10 mM; sodium chloride 5 mM; glucose 4 g/L; ammonium chloride 1 g/L; Feline Immunodeficiency Virus Myristoylated Matrix Protein 300 uM

sample_conditions_1: ionic strength: 5 mM; pH: 8; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 5 mM; pH: 8 pD; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_5isotropicsample_conditions_2
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_4isotropicsample_conditions_1
3D HNCACBsample_4isotropicsample_conditions_1
3D HNCOsample_4isotropicsample_conditions_1
3D HN(CA)COsample_4isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HMQCsample_3isotropicsample_conditions_2
2D 1H-13C HMQCsample_2isotropicsample_conditions_2
4D HMQC-NOESY-HMQCsample_2isotropicsample_conditions_2
4D HSQC-NOESY-HMQCsample_4isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

NMRFx, Johnson, One Moon Scientific - processing

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

TopSpin, Bruker Biospin - collection

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

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

NMR spectrometers:

  • Bruker DMX 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts