BMRB Entry 30739

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30739
MolProbity Validation Chart

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Title:
Solution NMR structure of the unmyristoylated 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.; Carter, H.; Ablan, S.; Freed, E.; Summers, M.
Citation:

Citation: Brown, J.; Summers, H.; Brown, L.; Marchant, J.; Canova, P.; O'Hern, C.; Abbott, S.; Nyaunu, C.; Maxwell, S.; Johnson, T.; Moser, M.; Carter, H.; Ablan, S.; Freed, E.; Summers, M.. "Structural and Mechanistic Studies of the Rare Myristoylation Signal of the Feline Immunodeficiency Virus"  J. Mol. Biol. 432, 4076-4091 (2020).
PubMed: 32442659

Assembly members:

Assembly members:
entity_1, polymer, 126 residues, 13988.002 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GNGQGRDWKMAIKRCSNVAV GVGGKSKKFGEGNFRWAIRM ANVSTGREPGDIPETLDQLR LVICDLQERREKFGSSKEID MAIVTLKVFAVAGLLNMTVS TAAAAENMYSQMGLDTRPHH HHHHHH

Data sets:
Data typeCount
13C chemical shifts472
15N chemical shifts124
1H chemical shifts611

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 126 residues - 13988.002 Da.

1   GLYASNGLYGLNGLYARGASPTRPLYSMET
2   ALAILELYSARGCYSSERASNVALALAVAL
3   GLYVALGLYGLYLYSSERLYSLYSPHEGLY
4   GLUGLYASNPHEARGTRPALAILEARGMET
5   ALAASNVALSERTHRGLYARGGLUPROGLY
6   ASPILEPROGLUTHRLEUASPGLNLEUARG
7   LEUVALILECYSASPLEUGLNGLUARGARG
8   GLULYSPHEGLYSERSERLYSGLUILEASP
9   METALAILEVALTHRLEULYSVALPHEALA
10   VALALAGLYLEULEUASNMETTHRVALSER
11   THRALAALAALAALAGLUASNMETTYRSER
12   GLNMETGLYLEUASPTHRARGPROHISHIS
13   HISHISHISHISHISHIS

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; Unmyristoylated Feline Immunodeficiency Virus Matrix Protein, [U-15N], 300 uM

sample_2: sodium phosphate 50 mM; DTT, [U-98% 2H], 10 mM; sodium chloride 5 mM; Unmyristoylated Feline Immunodeficiency Virus Matrix Protein 300 uM

sample_3: 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; Unmyristoylated Feline Immunodeficiency Virus Matrix Protein, [U-13C; U-15N], 300 uM

sample_4: 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; Unmyristoylated Feline Immunodeficiency Virus Matrix Protein, [U-13C], 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

sample_conditions_3: ionic strength: 5 mM; pH: 5; pressure: 1 atm; temperature: 298 K

sample_conditions_4: ionic strength: 5 mM; pH: 5 pD; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_2isotropicsample_conditions_2
2D 1H-1H NOESYsample_2isotropicsample_conditions_4
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_3
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_3
3D HNCOsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_3
3D HNCACBsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_3
2D 1H-15N HSQCsample_1isotropicsample_conditions_3
2D 1H-13 HMQCsample_4isotropicsample_conditions_2
4D HMQC-NOESY-HMQCsample_4isotropicsample_conditions_2
4D HSQC-NOESY-HMQCsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_3
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HN(CA)COsample_3isotropicsample_conditions_3
3D HN(CA)COsample_3isotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - collection

NMRFx, Johnson, One Moon Scientific - processing

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

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

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

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

NMR spectrometers:

  • Bruker DMX 600 MHz
  • Bruker DMX 500 MHz

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