BMRB Entry 26811

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26811

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Title:
13C Chemical shifts of free backbone carbonyls in bovine rhodopsin and Meta II
Deposition date:
2016-06-09
Original release date:
2016-06-16
Authors:
Kimata, Naoki; Pope, Andreyah; Sanchez-Reyes, Omar; Eilers, Markus; Opefi, Chikwado; Ziliox, Martine; Reeves, Philip; Smith, Steven
Citation:

Citation: Kimata, Naoki; Pope, Andreyah; Eilers, Markus; Opefi, Chikwado; Ziliox, Martine; Hirschfeld, Amiram; Zaitseva, Ekaterina; Vogel, Reiner; Sheves, Mordechai; Vogel, Reiner; Smith, Steven. "Retinal orientation and interactions in rhodopsin reveal a two-stage trigger mechanism for activation"  Nat. Commun. 7, 12683-12683 (2016).
PubMed: 27585742

Assembly members:

Assembly members:
Rhodopsin, polymer, 348 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: HEK293S   Vector: pACHrhoC

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Rhodopsin: MNGTEGPNFYVPFSNKTGVV RSPFEAPQYYLAEPWQFSML AAYMFLLIMLGFPINFLTLY VTVQHKKLRTPLNYILLNLA VADLFMVFGGFTTTLYTSLH GYFVFGPTGCNLEGFFATLG GEIALWSLVVLAIERYVVVC KPMSNFRFGENHAIMGVAFT WVMALACAAPPLVGWSRYIP EGMQCSCGIDYYTPHEETNN ESFVIYMFVVHFIIPLIVIF FCYGQLVFTVKEAAAQQQES ATTQKAEKEVTRMVIIMVIA FLICWLPYAGVAFYIFTHQG SDFGPIFMTIPAFFAKTSSV YNPVIYIMMNKQFRNCMVTT LCCGKNPLGDDEASTTVSKT ETSQVAPA

Data typeCount
13C chemical shifts11

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1rhodopsin1

Entities:

Entity 1, rhodopsin 348 residues - Formula weight is not available

1   METASNGLYTHRGLUGLYPROASNPHETYR
2   VALPROPHESERASNLYSTHRGLYVALVAL
3   ARGSERPROPHEGLUALAPROGLNTYRTYR
4   LEUALAGLUPROTRPGLNPHESERMETLEU
5   ALAALATYRMETPHELEULEUILEMETLEU
6   GLYPHEPROILEASNPHELEUTHRLEUTYR
7   VALTHRVALGLNHISLYSLYSLEUARGTHR
8   PROLEUASNTYRILELEULEUASNLEUALA
9   VALALAASPLEUPHEMETVALPHEGLYGLY
10   PHETHRTHRTHRLEUTYRTHRSERLEUHIS
11   GLYTYRPHEVALPHEGLYPROTHRGLYCYS
12   ASNLEUGLUGLYPHEPHEALATHRLEUGLY
13   GLYGLUILEALALEUTRPSERLEUVALVAL
14   LEUALAILEGLUARGTYRVALVALVALCYS
15   LYSPROMETSERASNPHEARGPHEGLYGLU
16   ASNHISALAILEMETGLYVALALAPHETHR
17   TRPVALMETALALEUALACYSALAALAPRO
18   PROLEUVALGLYTRPSERARGTYRILEPRO
19   GLUGLYMETGLNCYSSERCYSGLYILEASP
20   TYRTYRTHRPROHISGLUGLUTHRASNASN
21   GLUSERPHEVALILETYRMETPHEVALVAL
22   HISPHEILEILEPROLEUILEVALILEPHE
23   PHECYSTYRGLYGLNLEUVALPHETHRVAL
24   LYSGLUALAALAALAGLNGLNGLNGLUSER
25   ALATHRTHRGLNLYSALAGLULYSGLUVAL
26   THRARGMETVALILEILEMETVALILEALA
27   PHELEUILECYSTRPLEUPROTYRALAGLY
28   VALALAPHETYRILEPHETHRHISGLNGLY
29   SERASPPHEGLYPROILEPHEMETTHRILE
30   PROALAPHEPHEALALYSTHRSERSERVAL
31   TYRASNPROVALILETYRILEMETMETASN
32   LYSGLNPHEARGASNCYSMETVALTHRTHR
33   LEUCYSCYSGLYLYSASNPROLEUGLYASP
34   ASPGLUALASERTHRTHRVALSERLYSTHR
35   GLUTHRSERGLNVALALAPROALA

Samples:

sample_1: Rhodopsin, [1-13C; U-15N], 5 mg; sodium phosphate 2 mM; DDM 0.02%

sample_conditions_1: ionic strength: 2 mM; pH: 6; pressure: 1 atm; temperature: 190 K

Experiments:

NameSampleSample stateSample conditions
1D 13C, 15N REDORsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - processing

NMR spectrometers:

  • Bruker Avance 600 MHz