BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 26656

Title: Backbone 1H, 13C, 15N Chemical Shift Assignments for Full-length HIV-1 Transactivator of Transcription   PubMed: 26866386

Deposition date: 2015-09-11 Original release date: 2016-09-09

Authors: To, Vu; O'Neil, Joe

Citation: To, Vu; Dzananovic, Edis; McKenna, Sean; O'Neil, Joe. "The Dynamic Landscape of the Full-Length HIV-1 Transactivator of Transcription"  Biochemistry 55, 1314-1325 (2016).

Assembly members:
Tat101, polymer, 121 residues, 13670.4717 Da.

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

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

Entity Sequences (FASTA):
Tat101: MGSSHHHHHHSSGLVPRGSH MEPVDPRLEPWKHPGSQPKT ACTNCYCKKCCFHCQVCFIT KALGISYGRKKRRQRRRPPQ GSQTHQVSLSKQPASQPRGD PTGPKESKKKVERETETDPV D

Data sets:
Data typeCount
13C chemical shifts326
15N chemical shifts105
1H chemical shifts215

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Tat1011

Entities:

Entity 1, Tat101 121 residues - 13670.4717 Da.

Full-length HIV-1 Transactivator of transcription. This construct has a his-tag and thrombin digestion site on the N-terminal, accounting for the first 20 amino acids.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METGLUPROVALASPPROARGLEUGLUPRO
4   TRPLYSHISPROGLYSERGLNPROLYSTHR
5   ALACYSTHRASNCYSTYRCYSLYSLYSCYS
6   CYSPHEHISCYSGLNVALCYSPHEILETHR
7   LYSALALEUGLYILESERTYRGLYARGLYS
8   LYSARGARGGLNARGARGARGPROPROGLN
9   GLYSERGLNTHRHISGLNVALSERLEUSER
10   LYSGLNPROALASERGLNPROARGGLYASP
11   PROTHRGLYPROLYSGLUSERLYSLYSLYS
12   VALGLUARGGLUTHRGLUTHRASPPROVAL
13   ASP

Samples:

13C15NTat101: Tat101, [U-95% 13C; U-95% 15N], 0.5 mM; DSS 75 uM; acetic acid, [U-99% 2H], 10 mM; TCEP 2 mM

sample_conditions_1: pH: 4.0; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC13C15NTat101isotropicsample_conditions_1
3D HNCO13C15NTat101isotropicsample_conditions_1
3D HNCA13C15NTat101isotropicsample_conditions_1
3D HNHA13C15NTat101isotropicsample_conditions_1
3D CBCA(CO)NH13C15NTat101isotropicsample_conditions_1
3D HN(CA)CO13C15NTat101isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - data analysis, peak picking, processing

VNMR, Varian - collection

NMR spectrometers:

  • Varian INOVA 600 MHz

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