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 20079

Title: NMR solution structure of the loopregion Tyr67 - Leu77 of visual arrestin in complex with lightactivated rhodopsin   PubMed: 19835414

Authors: Feuerstein, Sophie; Hartmann, Rudolf; Koenig, Bernd

Citation: Feuerstein, Sophie; Pulvermuller, Alexander; Hartmann, Rudolf; Granzin, Joachim; Stoldt, Matthias; Henklein, Peter; Ernst, Oliver; Heck, Martin; Willbold, Dieter; Koenig, Bernd. "Helix formation in arrestin accompanies recognition of photoactivated rhodopsin."  Biochemistry 48, 10733-10742 (2009).

Assembly members:
Arr67_77, polymer, 11 residues, Formula weight is not available
rhodopsin, polymer, . residues, Formula weight is not available

Natural source:   Common Name: cow   Taxonomy ID: 9913   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Bos taurus

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
Arr67_77: YGQEDIDVMGL

Data sets:
Data typeCount
1H chemical shifts74

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Arr67_771
2rhodopsin2

Entities:

Entity 1, Arr67_77 11 residues - Formula weight is not available

1   TYRGLYGLNGLUASPILEASPVALMETGLY
2   LEU

Entity 2, rhodopsin - Formula weight is not available

Samples:

sample_1: Arr67_77 2 mM; rhodopsin 50 uM; sodium phosphate 10 mM; potassium chloride 20 mM; D2O 10 v/v; H2O 90 v/v

sample_2: Arr67_77 1 mM; sodium phosphate 10 mM; potassium chloride 20 mM; D2O 10 v/v; H2O 90 v/v

sample_conditions_1: pH: 6.6; pressure: 1.0 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
T-ROESYsample_2isotropicsample_conditions_1

Software:

VNMR, Varian - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

Molmol, Koradi, Billeter and Wuthrich - data analysis

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

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz

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