BMRB Entry 17017

Title:
Solution NMR Structure of (Ubiquitin thioesterase OTU1 EC3.1.2.-) from Mus musculus, Northeast Structural Genomics Consortium Target MmT2A
Deposition date:
2010-06-23
Original release date:
2010-07-26
Authors:
Chitayat, Seth; Gutmanas, Aleksandras; Lemak, Alexander; Yee, Adelinda; Bezsonova, Irina; Wu, Bin; Doherty, Ryan; Semesi, Anthony; Montelione, Gaetano; Arrowsmith, Cheryl; Dhe-Paganon, Sirano
Citation:

Citation: chitayat, seth. "Northeast Structural Genomics Consortium Target MmT2A"  To be published ., .-..

Assembly members:

Assembly members:
MmT2A, polymer, 86 residues, 9364.784 Da.

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28-MHL

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts346
15N chemical shifts87
1H chemical shifts585

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MmT2A1

Entities:

Entity 1, MmT2A 86 residues - 9364.784 Da.

1   TRPARGVALARGCYSLYSALALYSGLYGLY
2   THRHISLEULEUGLNGLYLEUSERSERARG
3   THRARGLEUARGGLULEUGLNGLYGLNILE
4   ALAALAILETHRGLYILEALAPROGLYSER
5   GLNARGILELEUVALGLYTYRPROPROGLU
6   CYSLEUASPLEUSERASPARGASPILETHR
7   LEUGLYASPLEUPROILEGLNSERGLYASP
8   METLEUILEVALGLUGLUASPGLNTHRARG
9   PROLYSALASERPROSER

Samples:

sample_1: MmT2A, [U-100% 13C; U-100% 15N], 1.1 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C arom NOESYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D H(C)CH-TOCSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
N15-edited NOESY-HSQCsample_1isotropicsample_conditions_1
C13-edited NOESY-HSQCsample_1isotropicsample_conditions_1

Software:

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinemen, structure solution

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis, refinement

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

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - data analysis

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

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

Molmol, Koradi, Billeter and Wuthrich - data analysis

MDDGUI v1.0, Gutmanas, Arrowsmith - processing

FMCGUI v2.3, Lemak, Arrowsmith - chemical shift assignment, refinement, structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinemen, structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAC29646 BAC29661 BAC35495
GB AAH99948 AAI39035
REF NP_848806
SP Q8CB27
AlphaFold Q8CB27

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