BMRB Entry 15955

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15955

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Title:
Green Proteorhodopsin
Deposition date:
2008-09-17
Original release date:
2009-01-28
Authors:
Shi, Lichi; Lake, Evelyn; Ahmed, Mumdooh; Zhang, Wurong; Whited, Gregg; Brown, Leonid; Ladizhansky, Vladimir
Citation:

Citation: Shi, Lichi; Lake, Evelyn; Ahmed, Mumdooh; Brown, Leonid; Ladizhansky, Vladimir. "Solid-state NMR study of proteorhodopsin in the lipid environment: secondary structure and dynamics."  Biochim. Biophys. Acta 1788, 2563-2574 (2009).
PubMed: 19799854

Assembly members:

Assembly members:
GPR, polymer, 255 residues, 29500 Da.
RETINAL, non-polymer, 284.436 Da.

Natural source:

Natural source:   Common Name: gamma proteobacterium   Taxonomy ID: 1236   Superkingdom: eubacteria   Kingdom: not available   Genus/species: not available gamma proteobacterium

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   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 shifts589
15N chemical shifts151

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PR1
2RE2

Entities:

Entity 1, PR 255 residues - 29500 Da.

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, RE - C20 H28 O - 284.436 Da.

1   RET

Samples:

sample_1: sodium chloride 50 mM; CHES 50 mM; DMPC 4 mg; DMPA 0.4 mg; GPR, [U-13C; U-15N], 9 mg; RET 0.09 mg

sample_2: CHES 50 mM; sodium chloride 50 mM; DMPC 5.4 mg; DMPA 0.6 mg; GPR, [U-13C; U-15N], 12 mg; RET 0.1 mg

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

Experiments:

NameSampleSample stateSample conditions
2D CC SPC53sample_1solidsample_conditions_1
3D NCACXsample_1solidsample_conditions_1
3D NCOCXsample_1solidsample_conditions_1
3D CONCAsample_1solidsample_conditions_1
3D CAN(CO)CAsample_1solidsample_conditions_1
2D CC SPC53sample_2solidsample_conditions_1
3D NCACXsample_2solidsample_conditions_1
3D NCOCXsample_2solidsample_conditions_1
3D CONCAsample_2solidsample_conditions_1
3D CAN(CO)CAsample_2solidsample_conditions_1

Software:

NMRPipe, Delaglio, Zhengrong and Bax - processing

TOPSPIN, Bruker Biospin - collection

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

BMRB 17327 17817
PDB
GB AAG10475 AAK30175 AAK30176 AAK30181 AAK30183
SP Q9F7P4
AlphaFold Q9F7P4