BMRB Entry 30285

Title:
Solution-state NMR structural ensemble of human Tsg101 UEV in complex with tenatoprazole
Deposition date:
2017-04-21
Original release date:
2017-11-10
Authors:
Strickland, Madeleine; Ehrlich, Lorna; Watanabe, Susan; Khan, Mahfuz; Strub, Marie-Paule; Luan, Chi-Hao; Powell, Michael; Leis, Jonathan; Tjandra, Nico; Carter, Carol
Citation:

Citation: Strickland, Madeleine; Ehrlich, Lorna; Watanabe, Susan; Khan, Mahfuz; Strub, Marie-Paule; Luan, Chi-Hao; Powell, Michael; Leis, Jonathan; Tjandra, Nico; Carter, Carol. "Tsg101 chaperone function revealed by HIV-1 assembly inhibitors."  Nat. Commun. 8, 1391-1391 (2017).
PubMed: 29123089

Assembly members:

Assembly members:
entity_1, polymer, 145 residues, 16559.207 Da.
entity_4N1, non-polymer, 331.413 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-28B

Data sets:
Data typeCount
13C chemical shifts521
15N chemical shifts143
1H chemical shifts1078

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 145 residues - 16559.207 Da.

1   GLYALAVALSERGLUSERGLNLEULYSLYS
2   METVALSERLYSTYRLYSTYRARGASPLEU
3   THRVALARGGLUTHRVALASNVALILETHR
4   LEUTYRLYSASPLEULYSPROVALLEUASP
5   SERTYRVALPHEASNASPGLYSERSERARG
6   GLULEUMETASNLEUTHRGLYTHRILEPRO
7   VALPROTYRARGGLYASNTHRTYRASNILE
8   PROILECYSLEUTRPLEULEUASPTHRTYR
9   PROTYRASNPROPROILECYSPHEVALLYS
10   PROTHRSERSERMETTHRILELYSTHRGLY
11   LYSHISVALASPALAASNGLYLYSILETYR
12   LEUPROTYRLEUHISGLUTRPLYSHISPRO
13   GLNSERASPLEULEUGLYLEUILEGLNVAL
14   METILEVALVALPHEGLYASPGLUPROPRO
15   VALPHESERARGPRO

Entity 2, entity_2 - C16 H19 N4 O2 S - 331.413 Da.

1   4N1

Samples:

sample_2: Tenatoprazole 0.6 mM; Tsg101, [U-13C; U-15N], 0.6 mM; potassium phosphate 20 mM; sodium chloride 50 mM

sample_1: Tenatoprazole 0.6 mM; Tsg101, [U-98% 13C; U-98% 15N], 0.6 mM; potassium phosphate 20 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 5.8; pressure: 1 atm; temperature: 300 K

sample_conditions_2: ionic strength: 0.1 mM; pH: 5.8 pH*; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_2
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_2
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_2
3D 1H-13C-12C filtered NOESY aliphaticsample_1isotropicsample_conditions_2
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1

Software:

Analysis v2.4.2, CCPN - chemical shift assignment, data analysis, peak picking

Gaussian v9, Gaussian, Inc. - geometry optimization

NMRDraw v8.2, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRPipe v8.2, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

PSVS v1.5, Bhattacharya and Montelione - data analysis

TALOS-N v4.12, Yang Shen and Ad Bax - data analysis

TOPSPIN v3.0, Bruker Biospin - collection

X-PLOR NIH v2.37.7, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz

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