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 15587

Title: 1H, 13C and 15N resonance assignment of Urm1 from Trypanosoma.brucei   PubMed: 19636925

Deposition date: 2007-12-11 Original release date: 2008-03-31

Authors: Zhang, Wen; Ding, Husheng; Zhang, Jiahai; Tu, xiaoming

Citation: Zhang, Wen; Ding, Husheng; Zhang, Jiahai; Tu, Xiaoming. "1H, 13C and 15N resonance assignment of Urm1 from Trypanosoma brucei"  Biomol. NMR Assignments 2, 59-60 (2008).

Assembly members:
ubiquitin-related_modifier, polymer, 110 residues, Formula weight is not available

Natural source:   Common Name: Trypanosoma brucei   Taxonomy ID: 5691   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Trypanosoma brucei

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: PET-22b(+)

Entity Sequences (FASTA):
ubiquitin-related_modifier: MSNHNHITVQFAGGCELLFA KQTSLQLDGVVPTGTNLNGL VQLLKTNYVKERPDLLVDQT GQTLRPGILVLVNSCDAEVV GGMDYVLNDGDTVEFISTLH GGLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts397
15N chemical shifts98
1H chemical shifts617

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1subunit 11

Entities:

Entity 1, subunit 1 110 residues - Formula weight is not available

1   METSERASNHISASNHISILETHRVALGLN
2   PHEALAGLYGLYCYSGLULEULEUPHEALA
3   LYSGLNTHRSERLEUGLNLEUASPGLYVAL
4   VALPROTHRGLYTHRASNLEUASNGLYLEU
5   VALGLNLEULEULYSTHRASNTYRVALLYS
6   GLUARGPROASPLEULEUVALASPGLNTHR
7   GLYGLNTHRLEUARGPROGLYILELEUVAL
8   LEUVALASNSERCYSASPALAGLUVALVAL
9   GLYGLYMETASPTYRVALLEUASNASPGLY
10   ASPTHRVALGLUPHEILESERTHRLEUHIS
11   GLYGLYLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: ubiquitin-related modifier 0.8-1 mM; NaH2PO4 50 mM; NaCL 100 mM; EDTA 1.5 mM; D2O, [U-100% 2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker DMX 600 MHz

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