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 25825

Title: UBL protein

Deposition date: 2015-09-23 Original release date: 2016-07-18

Authors: Chen, Xiang; Walters, Kylie

Citation: Chen, Xiang; Walters, Kylie. "UBL protein"  Not known ., .-..

Assembly members:
UBL_protein, polymer, 99 residues, Formula weight is not available

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

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

Entity Sequences (FASTA):
UBL_protein: MVSLTFKNFKKEKVPLDLEP SNTILETKTKLAQSISCEES QIKLIYSGKVLQDSKTVSEC GLKDGDQVVFMVSQKKSTDP NSSSVDKLAAALEHHHHHH

Data sets:
Data typeCount
13C chemical shifts404
15N chemical shifts98
1H chemical shifts675

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1UBL protein, 11
2UBL protein, 21

Entities:

Entity 1, UBL protein, 1 99 residues - Formula weight is not available

1   METVALSERLEUTHRPHELYSASNPHELYS
2   LYSGLULYSVALPROLEUASPLEUGLUPRO
3   SERASNTHRILELEUGLUTHRLYSTHRLYS
4   LEUALAGLNSERILESERCYSGLUGLUSER
5   GLNILELYSLEUILETYRSERGLYLYSVAL
6   LEUGLNASPSERLYSTHRVALSERGLUCYS
7   GLYLEULYSASPGLYASPGLNVALVALPHE
8   METVALSERGLNLYSLYSSERTHRASPPRO
9   ASNSERSERSERVALASPLYSLEUALAALA
10   ALALEUGLUHISHISHISHISHISHIS

Samples:

sample_1: UBL protein, [U-100% 13C; U-100% 15N], 0.7 mM; potassium phosphate 20 mM; sodium chloride 50 mM; DTT 2 mM; sodium azide 0.1%

sample_2: UBL protein, [U-100% 13C; U-100% 15N], 0.7 mM; potassium phosphate 20 mM; sodium chloride 50 mM; DTT 2 mM; sodium azide 0.1%

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
3D HCCH-TCOSYsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz

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