BMRB Entry 25573

Title:
NMR Structure of the Myristylated Feline Immunodeficiency Virus Matrix Protein
Deposition date:
2015-04-15
Original release date:
2015-05-26
Authors:
Brown, Lola; Cox, Cassiah; Button, Ryan; Baptiste, Janae; Bahlow, Kennedy; Spurrier, Vaughn; Luttge, Benjamin; Kuo, Lillian; Freed, Eric; Summers, Michael; Kyser, Jenna; Summers, Holly
Citation:

Citation: Brown, Lola; Cox, Cassiah; Baptiste, Janae; Summers, Holly; Button, Ryan; Bahlow, Kennedy; Spurrier, Vaughn; Kyser, Jenna; Luttge, Benjamin; Kuo, Lillian; Freed, Eric; Summers, Michael. "NMR structure of the myristylated feline immunodeficiency virus matrix protein"  Viruses 7, 2210-2229 (2015).
PubMed: 25941825

Assembly members:

Assembly members:
Feline_Immunodeficiency_Virus_Matrix_Protein, polymer, 135 residues, 14729.074 Da.

Natural source:

Natural source:   Common Name: domestic cat   Taxonomy ID: 9685   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Felis catus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET11/pET17

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts321
15N chemical shifts120
1H chemical shifts560

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Feline Immunodeficiency Virus Matrix Protein1

Entities:

Entity 1, Feline Immunodeficiency Virus Matrix Protein 135 residues - 14729.074 Da.

1   MYRGLYASNGLYALASERARGASPTRPLYS
2   METALAILELYSARGCYSSERASNVALALA
3   VALGLYVALGLYGLYLYSSERLYSLYSPHE
4   GLYGLUGLYASNPHEARGTRPALAILEARG
5   METALAASNVALSERTHRGLYARGGLUPRO
6   GLYASPILEPROGLUTHRLEUASPGLNLEU
7   ARGLEUVALILECYSASPLEUGLNGLUARG
8   ARGGLULYSPHEGLYSERSERLYSGLUILE
9   ASPMETALAILEVALTHRLEULYSVALPHE
10   ALAVALALAGLYLEULEUASNMETTHRVAL
11   SERTHRALAALAALAALAGLUASNMETTYR
12   SERGLNMETGLYLEUASPTHRARGPROSER
13   METLYSGLUALAGLYGLYLYSGLUGLUGLY
14   PROPROGLNALATYR

Samples:

90_H2O-15N_labeled: sodium phosphate 50 mM; sodium chloride 150 mM; DTT 10 mM; ammonium chloride, [U-99% 15N], 1 g/L; glucose 4 g/L; MYRISTIC ACID 0.5 mg/mL; H2O 90%; D2O 10%; Feline Immunodeficiency Virus Matrix Protein, [U-90% 15N], mM

D2O-13C: sodium phosphate 50 mM; sodium chloride 150 mM; DTT 10 mM; glucose, [U-100% 13C], 4 g/L; ammonium chloride 1 g/L; MYRISTIC ACID 0.5 mg/mL; D2O 100%; Feline Immunodeficiency Virus Matrix Protein, [U-100% 13C], mM

D2O-13C_1: sodium phosphate 50 mM; sodium chloride 150 mM; DTT 10 mM; glucose, [U-100% 13C], 4 g/L; ammonium chloride 1 g/L; MYRISTIC ACID 0.5 mg/mL; D2O 100%; Feline Immunodeficiency Virus Matrix Protein, [U-100% 13C], mM

D2O-13C_2: sodium phosphate 50 mM; sodium chloride 150 mM; DTT 10 mM; glucose, [U-100% 13C], 4 g/L; ammonium chloride 1 g/L; MYRISTIC ACID 0.5 mg/mL; D2O 100%; Feline Immunodeficiency Virus Matrix Protein, [U-100% 13C], mM

90_H2O-15N_labeled_1: sodium phosphate 50 mM; sodium chloride 150 mM; DTT 10 mM; ammonium chloride, [U-99% 15N], 1 g/L; glucose 4 g/L; MYRISTIC ACID 0.5 mg/mL; H2O 90%; D2O 10%; Feline Immunodeficiency Virus Matrix Protein, [U-90% 15N], mM

standard: ionic strength: 150 mM; pH: 7; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
15N-1HN HSQC90_H2O-15N_labeled_1isotropicstandard
13C-1HN HNCA90_H2O-15N_labeledisotropicstandard
13C-1HN HN(CO)CA90_H2O-15N_labeledisotropicstandard
CBCANH90_H2O-15N_labeledisotropicstandard
CBCA(CO)NH90_H2O-15N_labeledisotropicstandard
CARBON-NITROGEN NOESY (CNNOE)90_H2O-15N_labeledisotropicstandard
15N EDITED 3D NOESY90_H2O-15N_labeled_1isotropicstandard
1H-13C HMQCD2O-13C_2isotropicstandard
CARBON CARBON NOSEY (CCNOE)D2O-13C_2isotropicstandard
1H-1H NOESYD2O-13Cisotropicstandard
13C-1H HMQC NOESYD2O-13Cisotropicstandard

Software:

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

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

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

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker DMX 800 MHz
  • Bruker DMX 600 MHz

Related Database Links:

PDB
EMBL CAA40317
GB AAB59936
REF NP_040972
SP P16087
AlphaFold P16087

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