BMRB Entry 17817

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17817

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Green Proteorhodopsin - Deuterated
Deposition date:
2011-07-29
Original release date:
2011-10-25
Authors:
Ward, Meaghan; Shi, Lichi; Lake, Evelyn; Krishnamurthy, Sridevi; Hutchins, Howard; Brown, Leonid; Ladizhansky, Vladimir
Citation:

Citation: Ward, Meaghan; Shi, Lichi; Lake, Evelyn; Krishnamurthy, Sridevi; Hutchins, Howard; Brown, Leonid; Ladizhansky, Vladimir. "Proton-detected solid-state NMR reveals intramembrane polar networks in a seven-helical transmembrane protein proteorhodopsin."  J. Am. Chem. Soc. 133, 17434-17443 (2011).
PubMed: 21919530

Assembly members:

Assembly members:
GPR, polymer, 255 residues, Formula weight is not available
RET, non-polymer, 284.436 Da.

Natural source:

Natural source:   Common Name: Gamma proteobacteria   Taxonomy ID: 1236   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Gamma proteobacteria

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21   Vector: NA

Entity Sequences (FASTA):

Entity Sequences (FASTA):
GPR: MKLLLILGSVIALPTFAAGG GDLDASDYTGVSFWLVTAAL LASTVFFFVERDRVSAKWKT SLTVSGLVTGIAFWHYMYMR GVWIETGDSPTVFRYIDWLL TVPLLICEFYLILAAATNVA GSLFKKLLVGSLVMLVFGYM GEAGIMAAWPAFIIGCLAWV YMIYELWAGEGKSACNTASP AVQSAYNTMMYIIIFGWAIY PVGYFTGYLMGDGGSALNLN LIYNLADFVNKILFGLIIWN VAVKESSNAHHHHHH

Data sets:
Data typeCount
13C chemical shifts195
15N chemical shifts74
1H chemical shifts74

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Green Proteorhodopsin1
2retinal2

Entities:

Entity 1, Green Proteorhodopsin 255 residues - Formula weight is not available

1   METLYSLEULEULEUILELEUGLYSERVAL
2   ILEALALEUPROTHRPHEALAALAGLYGLY
3   GLYASPLEUASPALASERASPTYRTHRGLY
4   VALSERPHETRPLEUVALTHRALAALALEU
5   LEUALASERTHRVALPHEPHEPHEVALGLU
6   ARGASPARGVALSERALALYSTRPLYSTHR
7   SERLEUTHRVALSERGLYLEUVALTHRGLY
8   ILEALAPHETRPHISTYRMETTYRMETARG
9   GLYVALTRPILEGLUTHRGLYASPSERPRO
10   THRVALPHEARGTYRILEASPTRPLEULEU
11   THRVALPROLEULEUILECYSGLUPHETYR
12   LEUILELEUALAALAALATHRASNVALALA
13   GLYSERLEUPHELYSLYSLEULEUVALGLY
14   SERLEUVALMETLEUVALPHEGLYTYRMET
15   GLYGLUALAGLYILEMETALAALATRPPRO
16   ALAPHEILEILEGLYCYSLEUALATRPVAL
17   TYRMETILETYRGLULEUTRPALAGLYGLU
18   GLYLYSSERALACYSASNTHRALASERPRO
19   ALAVALGLNSERALATYRASNTHRMETMET
20   TYRILEILEILEPHEGLYTRPALAILETYR
21   PROVALGLYTYRPHETHRGLYTYRLEUMET
22   GLYASPGLYGLYSERALALEUASNLEUASN
23   LEUILETYRASNLEUALAASPPHEVALASN
24   LYSILELEUPHEGLYLEUILEILETRPASN
25   VALALAVALLYSGLUSERSERASNALAHIS
26   HISHISHISHISHIS

Entity 2, retinal - C20 H28 O - 284.436 Da.

1   RET

Samples:

sample_1: Deuterated Green Proteorhodopsin, [U-13C; U-15N; U-2H], 7 mg; sodium chloride 50 mM; CHES 50 mM; DMPC 3.6 mg; DMPA 0.4 mg; retinal 0.09 mg; D2O 60%; H2O 40%

sample_conditions_1: ionic strength: 100 mM; pH: 9; pressure: 1 atm; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
2D CC SPC53sample_1solidsample_conditions_1
3D CANHsample_1solidsample_conditions_1
3D CONHsample_1solidsample_conditions_1
3D DQCANHsample_1solidsample_conditions_1
3D DQCONHsample_1solidsample_conditions_1

Software:

NMRPipe, Delaglio, Zhengrong and Bax - processing

CARA, Keller and Wuthrich - chemical shift assignment

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

BMRB 15955 17327
PDB
GB AAG10475 AAK30175 AAK30176 AAK30181 AAK30183
SP Q9F7P4
AlphaFold Q9F7P4

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