BMRB Entry 5960

Title:
1H, 13C, 15N- Chemical Shift Assignments for Myristoylated HIV-1 Matrix Protein
Deposition date:
2003-10-01
Original release date:
2007-03-23
Authors:
Tang, Chun; Loeliger, Erin; Luncsford, Paz; Kinde, Isaac; Beckett, Dorothy; Summers, Michael
Citation:

Citation: Tang, Chun; Loeliger, Erin; Luncsford, Paz; Kinde, Isaac; Beckett, Dorothy; Summers, Michael. "From the Cover: Entropic switch regulates myristate exposure in the HIV-1 matrix protein"  Proc. Natl. Acad. Sci. U.S.A. 101, 517-522 (2004).
PubMed: 14699046

Assembly members:

Assembly members:
p17, polymer, 132 residues, 228.371 Da.

Natural source:

Natural source:   Common Name: HIV-1   Taxonomy ID: 11676   Superkingdom: Viruses   Kingdom: not available   Genus/species: Lentivirus Human immunodeficiency virus 1

Experimental source:

Experimental source:   Production method: recombinant technology

Data sets:
Data typeCount
1H chemical shifts581
15N chemical shifts130
13C chemical shifts500

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1matrix monomer1

Entities:

Entity 1, matrix monomer 132 residues - 228.371 Da.

1   MYRGLYALAARGALASERVALLEUSERGLY
2   GLYGLULEUASPLYSTRPGLULYSILEARG
3   LEUARGPROGLYGLYLYSLYSGLNTYRLYS
4   LEULYSHISILEVALTRPALASERARGGLU
5   LEUGLUARGPHEALAVALASNPROGLYLEU
6   LEUGLUTHRSERGLUGLYCYSARGGLNILE
7   LEUGLYGLNLEUGLNPROSERLEUGLNTHR
8   GLYSERGLUGLULEUARGSERLEUTYRASN
9   THRILEALAVALLEUTYRCYSVALHISGLN
10   ARGILEASPVALLYSASPTHRLYSGLUALA
11   LEUASPLYSILEGLUGLUGLUGLNASNLYS
12   SERLYSLYSLYSALAGLNGLNALAALAALA
13   ASPTHRGLYASNASNSERGLNVALSERGLN
14   ASNTYR

Samples:

sample_1: p17, [U-13C; U-15N], 0.2 mM; sodium phosophate buffer 50 mM; NaCl 50 mM; DTT 5 mM; DTT 5 mM

cond_1: pH: 5.5; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1not availablecond_1
2D 1H-13C HMQCsample_1not availablecond_1
2D 1H-1H NOESYsample_1not availablecond_1
3D 13C-edited HMQC-NOESYsample_1not availablecond_1
2D 13C-edited HMQC-NOESYsample_1not availablecond_1
4D 13C, 13C-edited HMQC-NOESY-HMQCsample_1not availablecond_1
3D 15N- edited NOESY-HSQCsample_1not availablecond_1
3D HNCAsample_1not availablecond_1
3D HN(CO)CAsample_1not availablecond_1
3D HNCOsample_1not availablecond_1

Software:

NMRPIPE - processing

NMRVIEW v5.0.4 - processing

NMR spectrometers:

  • Bruker AVANCE 800 MHz
  • Bruker AVANCE 600 MHz

Related Database Links:

BMRB 15114 15116 18715 18716 5316 7250 7267 7275 7309
PDB
DBJ BAF34641 BAG48474
EMBL CBI61180 CBI61181 CBI61182 CBI61183 CBI61184
GB AAA44987 AAB00898 AAB60571 AAC28445 AAC29216
SP P12493 P12497
AlphaFold P12493 P12497

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