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 15547

Title: Solution structure of ubiquitin domain N-terminal to S27a ribosome subunit from Giardia lamblia   PubMed: 17599068

Deposition date: 2007-11-07 Original release date: 2008-11-03

Authors: Catic, Andre; Sun, Zhen-Yu; Ratner, Daniel; Misaghi, Shahram; Spooner, Eric; Samuelson, John; Wagner, Gerhard; Ploegh, Hidde

Citation: Catic, Andre; Sun, Zhen-Yu; Ratner, Daniel; Misaghi, Shahram; Spooner, Eric; Samuelson, John; Wagner, Gerhard; Ploegh, Hidde. "Sequence and structure evolved separately in a ribosomal ubiquitin variant"  EMBO J. 26, 3474-3483 (2007).

Assembly members:
GlUb(S27a), polymer, 69 residues, 7307.402 Da.

Natural source:   Common Name: Giardia intestinalis   Taxonomy ID: 5741   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Giardia lamblia

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

Entity Sequences (FASTA):
GlUb(S27a): MLVIVRLQDQTLPFELPAGA RASQLSNLLSSSGMAFSLHT QGRVLSEAAELNDKMVIDAF VPADGAGLE

Data sets:
Data typeCount
13C chemical shifts265
15N chemical shifts66
1H chemical shifts456

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1GlUb(S27a)1

Entities:

Entity 1, GlUb(S27a) 69 residues - 7307.402 Da.

two C-terminal residues are from cloning artifact

1   METLEUVALILEVALARGLEUGLNASPGLN
2   THRLEUPROPHEGLULEUPROALAGLYALA
3   ARGALASERGLNLEUSERASNLEULEUSER
4   SERSERGLYMETALAPHESERLEUHISTHR
5   GLNGLYARGVALLEUSERGLUALAALAGLU
6   LEUASNASPLYSMETVALILEASPALAPHE
7   VALPROALAASPGLYALAGLYLEUGLU

Samples:

sample_1: GlUb(S27a), [U-99% 13C; U-99% 15N], 1 mM; potassium phosphate 10 mM; sodium chloride 100 mM; D2O 10%; H20 90%

sample_2: GlUb(S27a) 1 mM; potassium phosphate 10 mM; sodium chloride 100 mM; D2O 100%

sample_3: GlUb(S27a), [U-10% 13C], 1 mM; potassium phosphate 10 mM; sodium chloride 100 mM; D2O 100%

sample_conditions_1: ionic strength: 100 mM; pH: 6.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1

Software:

PROSA v3.7, Guntert - processing

CARA v1.8.2, Keller and Wuthrich - data analysis

RNMRTK v3, Stern and Hoch - processing

TALOS v2003.027.13.05, Cornilescu, Delaglio and Bax - data analysis

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance 750 MHz
  • Varian INOVA 500 MHz

Related Database Links:

PDB
GB EDO78147 ESU35090
REF XP_001705821

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