BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 18758

Title: Refined solution structure and dynamics of First Catalytic Cysteine Half-domain from mouse E1 enzyme   PubMed: 24211821

Authors: Jaremko, Mariusz; Jaremko, Lukasz; Nowakowski, Michal; Szczepanowski, Roman; Filipek, Renata; Wojciechowski, Marek; Bochtler, Matthias; Ejchart, Andrzej

Citation: Jaremko, Mariusz; Jaremko, ukasz; Nowakowski, Micha; Wojciechowski, Marek; Szczepanowski, Roman; Panecka, Renata; Zhukov, Igor; Bochtler, Matthias; Ejchart, Andrzej. "NMR structural studies of the first catalytic half-domain of ubiquitin activating enzyme."  J. Struct. Biol. 185, 69-78 (2014).

Assembly members:
entity, polymer, 112 residues, 12195.902 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Saccharomyces cerevisiae

Entity Sequences (FASTA):
entity: EFGEEMVLTDSNGEQPLSAM VSMVTKDNPGVVTCLDEARH GFETGDFVSFSEVQGMIQLN GCQPMEIKVLGPYTFSICDT SNFSDYIRGGIVSQVKVPKK ISFKSLPASLVE

Data sets:
Data typeCount
13C chemical shifts469
15N chemical shifts110
1H chemical shifts769
heteronuclear NOE values99
order parameters71
T1 relaxation values100
T2 relaxation values99

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1First Catalytic Cysteine Half-domain1

Entities:

Entity 1, First Catalytic Cysteine Half-domain 112 residues - 12195.902 Da.

1   GLUPHEGLYGLUGLUMETVALLEUTHRASP
2   SERASNGLYGLUGLNPROLEUSERALAMET
3   VALSERMETVALTHRLYSASPASNPROGLY
4   VALVALTHRCYSLEUASPGLUALAARGHIS
5   GLYPHEGLUTHRGLYASPPHEVALSERPHE
6   SERGLUVALGLNGLYMETILEGLNLEUASN
7   GLYCYSGLNPROMETGLUILELYSVALLEU
8   GLYPROTYRTHRPHESERILECYSASPTHR
9   SERASNPHESERASPTYRILEARGGLYGLY
10   ILEVALSERGLNVALLYSVALPROLYSLYS
11   ILESERPHELYSSERLEUPROALASERLEU
12   VALGLU

Samples:

sample_1: First Cysteine Catalytic Half-domain, [U-100% 13C; U-100% 15N], 1 mM; H2O 90 mM; D2O 10 mM

sample_2: First Cysteine Catalytic Half-domain, [U-100% 15N], 1 mM; H2O 90 mM; D2O 10 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH v2.26, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - peak picking

SPARKY, Goddard - chemical shift assignment

WhatIF, Vriend - refinement

NMR spectrometers:

  • Varian UnityPlus 500 MHz
  • Bruker Avance 700 MHz
  • Varian INOVA 400 MHz

Related Database Links:

PDB
DBJ BAA01433 BAC40121 BAC40405 BAE25369 BAE42599
GB AAH58630 AAI38201 AAI45985 EDL00743
REF NP_001129557 NP_001263245 NP_001263246 NP_033483
SP Q02053