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 18595

Title: Solid-state NMR 13C and 15N resonance assignments of a seven-transmembrane helical protein Anabaena Sensory Rhodopsin   PubMed: 22983928

Authors: Wang, Shenlin; Shi, Lichi; Brown, Leonid; Ladizhansky, Vladimir

Citation: Wang, Shenlin; Shi, Lichi; Okitsu, Takashi; Wada, Akimori; Brown, Leonid; Ladizhansky, Vladimir. "Solid-state NMR 13C and 15N resonance assignments of a seven-transmembrane helical protein Anabaena Sensory Rhodopsin"  Biomol. NMR Assign. 7, 253-256 (2013).

Assembly members:
ASR, polymer, 235 residues, Formula weight is not available

Natural source:   Common Name: Cyanobacteria   Taxonomy ID: 1172   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Anabaena variabilis

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
ASR: MNLESLLHWIYVAGMTIGAL HFWSLSRNPRGVPQYEYLVA MFIPIWSGLAYMAMAIDQGK VEAAGQIAHYARYIDWMVTT PLLLLSLSWTAMQFIKKDWT LIGFLMSTQIVVITSGLIAD LSERDWVRYLWYICGVCAFL IILWGIWNPLRAKTRTQSSE LANLYDKLVTYFTVLWIGYP IVWIIGPSGFGWINQTIDTF LFCLLPFFSKVGFSFLDLHG LRNLNDSRQHHHHHH

Data sets:
Data typeCount
13C chemical shifts963
15N chemical shifts223

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Anabeana sensory rhodopsin1

Entities:

Entity 1, Anabeana sensory rhodopsin 235 residues - Formula weight is not available

6X his-tagged C-terminal truncated at position 229 Anabeana sensory rhodospin

1   METASNLEUGLUSERLEULEUHISTRPILE
2   TYRVALALAGLYMETTHRILEGLYALALEU
3   HISPHETRPSERLEUSERARGASNPROARG
4   GLYVALPROGLNTYRGLUTYRLEUVALALA
5   METPHEILEPROILETRPSERGLYLEUALA
6   TYRMETALAMETALAILEASPGLNGLYLYS
7   VALGLUALAALAGLYGLNILEALAHISTYR
8   ALAARGTYRILEASPTRPMETVALTHRTHR
9   PROLEULEULEULEUSERLEUSERTRPTHR
10   ALAMETGLNPHEILELYSLYSASPTRPTHR
11   LEUILEGLYPHELEUMETSERTHRGLNILE
12   VALVALILETHRSERGLYLEUILEALAASP
13   LEUSERGLUARGASPTRPVALARGTYRLEU
14   TRPTYRILECYSGLYVALCYSALAPHELEU
15   ILEILELEUTRPGLYILETRPASNPROLEU
16   ARGALALYSTHRARGTHRGLNSERSERGLU
17   LEUALAASNLEUTYRASPLYSLEUVALTHR
18   TYRPHETHRVALLEUTRPILEGLYTYRPRO
19   ILEVALTRPILEILEGLYPROSERGLYPHE
20   GLYTRPILEASNGLNTHRILEASPTHRPHE
21   LEUPHECYSLEULEUPROPHEPHESERLYS
22   VALGLYPHESERPHELEUASPLEUHISGLY
23   LEUARGASNLEUASNASPSERARGGLNHIS
24   HISHISHISHISHIS

Samples:

sample_1: ASR, [U-100% 13C; U-100% 15N], w/w; DMPC, [U-100% 13C; U-100% 15N], w/w; DMPA, [U-100% 13C; U-100% 15N], w/w

sample_2: ASR, alternately labeled by 2-13C glycerol and U- 15N, w/w; DMPC, [U-100% 13C; U-100% 15N], w/w; DMPA, [U-100% 13C; U-100% 15N], w/w

sample_3: ASR, 1,3-C13-glycerol labeled and U-N15 labeled, w/w; DMPC, [U-100% 13C; U-100% 15N], w/w; DMPA, [U-100% 13C; U-100% 15N], w/w

sample_conditions_1: pH: 9.0; pressure: 1 atm; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
2D NCAsample_1solidsample_conditions_1
2D NCOsample_1solidsample_conditions_1
3D CONCAsample_1solidsample_conditions_1
3D NCACXsample_1solidsample_conditions_1
3D NCOCXsample_1solidsample_conditions_1
2D CC (DARR)sample_1solidsample_conditions_1
2D NCAsample_2solidsample_conditions_1
2D NCOsample_2solidsample_conditions_1
3D NCACXsample_2solidsample_conditions_1
3D NCOCXsample_2solidsample_conditions_1
2D CC (DARR)sample_2solidsample_conditions_1
2D NCAsample_3solidsample_conditions_1
2D NCOsample_3solidsample_conditions_1
3D NCACXsample_3solidsample_conditions_1
3D NCOCXsample_3solidsample_conditions_1
2D CC (DARR)sample_3solidsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMRPipe, Delaglio, Zhengrong and Bax - processing

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

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links: