BMRB Entry 26656

Name: Backbone 1H, 13C, 15N Chemical Shift Assignments for Full-length HIV-1 Transactivator of Transcription
Published: 2016-09-09

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26656

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

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

Deposition date:

2015-09-11

Original release date:

2016-09-09

Authors:

To, Vu; O'Neil, Joe

Citation:

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).
PubMed: 26866386

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28b

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	326
15N chemical shifts	105
1H chemical shifts	215

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Tat101	1

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

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

GLU

PRO

VAL

ASP

PRO

ARG

LEU

GLU

PRO

4

TRP

LYS

HIS

PRO

GLY

SER

GLN

PRO

LYS

THR

5

ALA

CYS

THR

ASN

CYS

TYR

CYS

LYS

CYS

6

CYS

PHE

HIS

CYS

GLN

VAL

CYS

PHE

ILE

THR

7

LYS

ALA

LEU

GLY

ILE

SER

TYR

GLY

ARG

LYS

8

LYS

ARG

GLN

ARG

PRO

GLN

9

GLY

SER

GLN

THR

HIS

GLN

VAL

SER

LEU

SER

10

LYS

GLN

PRO

ALA

SER

GLN

PRO

ARG

GLY

ASP

11

PRO

THR

GLY

PRO

LYS

GLU

SER

LYS

12

VAL

GLU

ARG

GLU

THR

GLU

THR

ASP

PRO

VAL

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	13C15NTat101	isotropic	sample_conditions_1
3D HNCO	13C15NTat101	isotropic	sample_conditions_1
3D HNCA	13C15NTat101	isotropic	sample_conditions_1
3D HNHA	13C15NTat101	isotropic	sample_conditions_1
3D CBCA(CO)NH	13C15NTat101	isotropic	sample_conditions_1
3D HN(CA)CO	13C15NTat101	isotropic	sample_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 HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks