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 30675

Title: Solution-state NMR structural ensemble of human Tsg101 UEV in complex with K63-linked diubiquitin

Deposition date: 2019-09-18 Original release date: 2021-03-12

Authors: Strickland, M.; Watanabe, S.; Bonn, S.; Camara, C.; Fushman, D.; Carter, C.; Tjandra, N.

Citation: Strickland, M.; Watanabe, S.; Bonn, S.; Camara, C.; Fushman, D.; Carter, C.; Tjandra, N.. "Dual Binding Modes of K63-Linked Diubiquitin Regulate Tsg101/ESCRT-I Recruitment"  .

Assembly members:
entity_1, polymer, 76 residues, 8604.845 Da.
entity_2, polymer, 77 residues, 8691.918 Da.
entity_3, polymer, 145 residues, 16633.352 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21

Entity Sequences (FASTA):
entity_1: MQIFVKTLTGKTITLEVEPS DTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYN IQRESTLHLVLRLRGG
entity_2: MQIFVKTLTGKTITLEVEPS DTIENVKAKIQDKEGIPPDQ QRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGGD
entity_3: MAVSESQLKKMVSKYKYRDL TVRETVNVITLYKDLKPVLD SYVFNDGSSRELMNLTGTIP VPYRGNTYNIPICLWLLDTY PYNPPICFVKPTSSMTIKTG KHVDANGKIYLPYLHEWKHP QSDLLGLIQVMIVVFGDEPP VFSRP

Data sets:
Data typeCount
15N chemical shifts271
1H chemical shifts271

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22
3entity_33

Entities:

Entity 1, entity_1 76 residues - 8604.845 Da.

1   METGLNILEPHEVALLYSTHRLEUTHRGLY
2   LYSTHRILETHRLEUGLUVALGLUPROSER
3   ASPTHRILEGLUASNVALLYSALALYSILE
4   GLNASPLYSGLUGLYILEPROPROASPGLN
5   GLNARGLEUILEPHEALAGLYLYSGLNLEU
6   GLUASPGLYARGTHRLEUSERASPTYRASN
7   ILEGLNARGGLUSERTHRLEUHISLEUVAL
8   LEUARGLEUARGGLYGLY

Entity 2, entity_2 77 residues - 8691.918 Da.

1   METGLNILEPHEVALLYSTHRLEUTHRGLY
2   LYSTHRILETHRLEUGLUVALGLUPROSER
3   ASPTHRILEGLUASNVALLYSALALYSILE
4   GLNASPLYSGLUGLYILEPROPROASPGLN
5   GLNARGLEUILEPHEALAGLYLYSGLNLEU
6   GLUASPGLYARGTHRLEUSERASPTYRASN
7   ILEGLNLYSGLUSERTHRLEUHISLEUVAL
8   LEUARGLEUARGGLYGLYASP

Entity 3, entity_3 145 residues - 16633.352 Da.

1   METALAVALSERGLUSERGLNLEULYSLYS
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

Samples:

sample_1: Tsg101 UEV domain, [U-98% 15N], 200 uM; K63-linked diubiquitin, distal domain 200 uM; K63-linked diubiquitin, proximal domain 200 uM; potassium phosphate 20 mM; sodium chloride 50 mM

sample_2: Tsg101 UEV domain 200 uM; K63-linked diubiquitin, distal domain, [U-98% 15N], 200 uM; K63-linked diubiquitin, proximal domain 200 uM; potassium phosphate 20 mM; sodium chloride 50 mM

sample_3: Tsg101 UEV domain 200 uM; K63-linked diubiquitin, distal domain 200 uM; K63-linked diubiquitin, proximal domain, [U-98% 15N], 200 uM; potassium phosphate 20 mM; sodium chloride 50 mM

sample_4: Tsg101 UEV domain, [U-98% 15N], 125 uM; K63-linked diubiquitin, distal domain 125 uM; K63-linked diubiquitin, proximal domain 125 uM; potassium phosphate 20 mM; sodium chloride 50 mM

sample_5: Tsg101 UEV domain, [U-98% 15N], 125 uM; K63-linked diubiquitin, distal domain 125 uM; K63-linked diubiquitin, proximal domain 125 uM; potassium phosphate 20 mM; sodium chloride 50 mM

sample_6: Tsg101 UEV domain, [U-98% 15N], 125 uM; K63-linked diubiquitin, distal domain 125 uM; K63-linked diubiquitin, proximal domain 125 uM; potassium phosphate 20 mM; sodium chloride 50 mM

sample_7: Tsg101 UEV domain, [U-98% 15N], 125 uM; K63-linked diubiquitin, distal domain 125 uM; K63-linked diubiquitin, proximal domain 125 uM; potassium phosphate 20 mM; sodium chloride 50 mM

sample_8: Tsg101 UEV domain, [U-98% 15N], 200 uM; potassium phosphate 20 mM; sodium chloride 50 mM

sample_9: K63-linked diubiquitin, distal domain, [U-98% 15N], 200 uM; K63-linked diubiquitin, proximal domain 200 uM; potassium phosphate 20 mM; sodium chloride 50 mM

sample_10: K63-linked diubiquitin, distal domain 200 uM; K63-linked diubiquitin, proximal domain, [U-98% 15N], 200 uM; 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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_4isotropicsample_conditions_1
2D 1H-15N HSQCsample_5anisotropicsample_conditions_1
2D 1H-15N HSQCsample_6isotropicsample_conditions_1
2D 1H-15N HSQCsample_7anisotropicsample_conditions_1
2D 1H-15N HSQCsample_8isotropicsample_conditions_1
2D 1H-15N HSQCsample_9isotropicsample_conditions_1
2D 1H-15N HSQCsample_10isotropicsample_conditions_1

Software:

NMRPipe v9.5, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TopSpin v3.0, Bruker Biospin - collection

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

X-PLOR NIH v2.51, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

NMR spectrometers:

  • Bruker AVANCE 600 MHz
  • Bruker AVANCE 800 MHz

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