BMRB Entry 19150

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19150

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Title:
1H, 15N, and 13C Chemical Shift Assignments of the Light-activated State of a Cyanobacterial GAF Domain (NpF2164-GAF3)
Deposition date:
2013-04-08
Original release date:
2013-08-15
Authors:
Lim, Sunghyuk; Rockwell, Nathan; Martin, Shelley; Lagarias, J.; Ames, James
Citation:

Citation: Lim, Sunghyuk; Rockwell, Nathan; Martin, Shelley; Lagarias, J. Clark; Ames, James. "(1)H, (15)N, and (13)C chemical shift assignments of cyanobacteriochrome NpF2164g3 in the photoproduct state."  Biomol. NMR Assignments ., .-. (2013).
PubMed: 23749453

Assembly members:

Assembly members:
NpF2164-GAF3, polymer, 223 residues, Formula weight is not available
PHYCOCYANOBILIN, non-polymer, 588.694 Da.

Natural source:

Natural source:   Common Name: cyanobacteria   Taxonomy ID: 272131   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Nostoc punctiforme

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NpF2164-GAF3: MGSSHHHHHHSSGLVPRGSH MERERTVFGIIEKIGQATDL RTLFRTATQELRRFLKCDRV VVYQFHPDWSGEVIAESVGA GWSSLVEMQEQDGILKTGLI SSERCNIKDYGSPVKADADT YLKETQGGMYAKGTRFRKVN DISAAGFSSCYLESLEKFQA KAYIIVPVFRAGNLWGLLAA YQNSEVRQWTEEEAGALLQI AEPLSIALQQAEYIEQLRLK NLE

Data sets:
Data typeCount
13C chemical shifts509
15N chemical shifts179
1H chemical shifts356

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NpF2164-GAF31
2entity_CYC2

Entities:

Entity 1, NpF2164-GAF3 223 residues - Formula weight is not available

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METGLUARGGLUARGTHRVALPHEGLYILE
4   ILEGLULYSILEGLYGLNALATHRASPLEU
5   ARGTHRLEUPHEARGTHRALATHRGLNGLU
6   LEUARGARGPHELEULYSCYSASPARGVAL
7   VALVALTYRGLNPHEHISPROASPTRPSER
8   GLYGLUVALILEALAGLUSERVALGLYALA
9   GLYTRPSERSERLEUVALGLUMETGLNGLU
10   GLNASPGLYILELEULYSTHRGLYLEUILE
11   SERSERGLUARGCYSASNILELYSASPTYR
12   GLYSERPROVALLYSALAASPALAASPTHR
13   TYRLEULYSGLUTHRGLNGLYGLYMETTYR
14   ALALYSGLYTHRARGPHEARGLYSVALASN
15   ASPILESERALAALAGLYPHESERSERCYS
16   TYRLEUGLUSERLEUGLULYSPHEGLNALA
17   LYSALATYRILEILEVALPROVALPHEARG
18   ALAGLYASNLEUTRPGLYLEULEUALAALA
19   TYRGLNASNSERGLUVALARGGLNTRPTHR
20   GLUGLUGLUALAGLYALALEULEUGLNILE
21   ALAGLUPROLEUSERILEALALEUGLNGLN
22   ALAGLUTYRILEGLUGLNLEUARGLEULYS
23   ASNLEUGLU

Entity 2, entity_CYC - C33 H40 N4 O6 - 588.694 Da.

1   CYC

Samples:

sample_1: NpF2164-GAF3, [U-99% 15N], 0.7 mM; sodium phosphate 10 mM; TCEP, [U-2H], 1.2 mM; D2O, [U-99% 2H], 7%; H2O 93%

sample_2: NpF2164-GAF3, [U-99% 13C; U-99% 15N], 0.7 mM; potassium phosphate 10 mM; TCEP, [U-2H], 1.2 mM; D2O, [U-99% 2H], 7%; H2O 93%

sample_conditions_1: ionic strength: 25 mM; pH: 7.4; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCACOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 19629

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