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 17327

Title: Not known   PubMed: 22034093

Authors: Reckel, Sina; Gottstein, Daniel; Stehle, Jochen; Loehr, Frank; Takeda, Mitsuhiro; Silvers, Robert; Kainosho, Masatsune; Glaubitz, Clemens; Bernhard, Frank; Schwalbe, Harald; Guntert, Peter; Doetsch, Volker

Citation: Reckel, Sina; Gottstein, Daniel; Stehle, Jochen; Lohr, Frank; Verhoefen, Mirka-Kristin; Takeda, Mitsuhiro; Silvers, Robert; Kainosho, Masatsune; Glaubitz, Clemens; Wachtveitl, Josef; Bernhard, Frank; Schwalbe, Harald; Guntert, Peter; Dotsch, Volker. "Solution NMR structure of proteorhodopsin."  Angew. Chem. Int. Ed. Engl. 50, 11942-11946 (2011).

Assembly members:
proteorhodopsin, polymer, 243 residues, Formula weight is not available

Natural source:   Common Name: Gamma-proteobacterium   Taxonomy ID: 86473   Superkingdom: bacteria   Kingdom: not available   Genus/species: not available Gamma Proteobacterial sp.

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free

Entity Sequences (FASTA):
proteorhodopsin: MGGGDLDASDYTGVSFWLVT AALLASTVFFFVERDRVSAK WKTSLTVSGLVTGIAFWHYM YMRGVWIETGDSPTVFRYID WLLTVPLLICEFYLILAAAT NVAGSLFKKLLVGSLVMLVF GYMGEAGIMAAWPAFIIGCL AWVYMIYELWAGEGKSACNT ASPAVQSAYNTMMYIIIFGW AIYPVGYFTGYLMGDGGSAL NLNLIYNLADFVNXILFGLI IWNVAVKESSNAPGGGSHHH HHH

Data sets:
Data typeCount
13C chemical shifts783
15N chemical shifts223
1H chemical shifts998

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1proteorhodopsin1

Entities:

Entity 1, proteorhodopsin 243 residues - Formula weight is not available

1   METGLYGLYGLYASPLEUASPALASERASP
2   TYRTHRGLYVALSERPHETRPLEUVALTHR
3   ALAALALEULEUALASERTHRVALPHEPHE
4   PHEVALGLUARGASPARGVALSERALALYS
5   TRPLYSTHRSERLEUTHRVALSERGLYLEU
6   VALTHRGLYILEALAPHETRPHISTYRMET
7   TYRMETARGGLYVALTRPILEGLUTHRGLY
8   ASPSERPROTHRVALPHEARGTYRILEASP
9   TRPLEULEUTHRVALPROLEULEUILECYS
10   GLUPHETYRLEUILELEUALAALAALATHR
11   ASNVALALAGLYSERLEUPHELYSLYSLEU
12   LEUVALGLYSERLEUVALMETLEUVALPHE
13   GLYTYRMETGLYGLUALAGLYILEMETALA
14   ALATRPPROALAPHEILEILEGLYCYSLEU
15   ALATRPVALTYRMETILETYRGLULEUTRP
16   ALAGLYGLUGLYLYSSERALACYSASNTHR
17   ALASERPROALAVALGLNSERALATYRASN
18   THRMETMETTYRILEILEILEPHEGLYTRP
19   ALAILETYRPROVALGLYTYRPHETHRGLY
20   TYRLEUMETGLYASPGLYGLYSERALALEU
21   ASNLEUASNLEUILETYRASNLEUALAASP
22   PHEVALASNLYRILELEUPHEGLYLEUILE
23   ILETRPASNVALALAVALLYSGLUSERSER
24   ASNALAPROGLYGLYGLYSERHISHISHIS
25   HISHISHIS

Samples:

sample_1: proteorhodopsin, [U-13C; U-15N], 300 uM; H2O 90%; D2O 10%; NaOAc 25 mM; DTT 2 mM; diC7PC 2%

sample_2: proteorhodopsin, [U-13C; U-15N; U-2H], 300 uM; H2O 90%; D2O 10%; NaOAc 25 mM; DTT 2 mM; diC7PC 2%

sample_3: proteorhodopsin, [U-15N; U-2H], 300 uM; H2O 90%; D2O 10%; NaOAc 25 mM; DTT 2 mM; diC7PC 2%

sample_conditions_1: ionic strength: 0.025 M; pH: 5; pressure: 1 atm; temperature: 323 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1

Software:

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

TOPSPIN, Bruker Biospin - collection, data analysis, processing

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz
  • Bruker Avance 950 MHz

Related Database Links:

EMBL AAG10475.1
UNP Q9F7P4
BMRB 15955 17817
PDB
GB AAG10475 AAK30175 AAK30176 AAK30183 AAK30184
SP Q9F7P4