BMRB Entry 16600

Title:
Backbone resonance assignments of cgGFP
Deposition date:
2009-11-09
Original release date:
2010-09-28
Authors:
Feng, Yingang; Wang, Jinfeng
Citation:

Citation: Titushin, Maxim; Feng, Yingang; Stepanyuk, Galina; Li, Yang; Markova, Svetlana; Golz, Stefan; Wang, Bi-Cheng; Lee, John; Wang, Jinfeng; Vysotski, Eugene; Liu, Zhi-Jie. "NMR-derived topology of a GFP-photoprotein energy transfer complex."  J. Biol. Chem. 285, 40891-40900 (2010).
PubMed: 20926380

Assembly members:

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

Natural source:

Natural source:   Common Name: Clytia gregaria   Taxonomy ID: 27801   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Clytia gregaria

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET19b

Data sets:
Data typeCount
13C chemical shifts612
15N chemical shifts209
1H chemical shifts361

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1gfp1

Entities:

Entity 1, gfp 235 residues - Formula weight is not available

1   METTHRALALEUTHRGLUGLYALALYSLEU
2   PHEGLULYSGLUILEPROTYRILETHRGLU
3   LEUGLUGLYASPVALGLUGLYMETLYSPHE
4   ILEILELYSGLYGLUGLYTHRGLYASPALA
5   THRTHRGLYTHRILELYSALALYSTYRILE
6   CYSTHRTHRGLYASPLEUPROVALPROTRP
7   ALATHRILELEUSERSERLEUSERTYRGLY
8   VALPHECYSPHEALALYSTYRPROARGHIS
9   ILEALAASPPHEPHELYSSERTHRGLNPRO
10   ASPGLYTYRSERGLNASPARGILEILESER
11   PHEASPASNASPGLYGLNTYRASPVALLYS
12   ALALYSVALTHRTYRGLUASNGLYTHRLEU
13   TYRASNARGVALTHRVALLYSGLYTHRGLY
14   PHELYSSERASNGLYASNILELEUGLYMET
15   ARGVALLEUTYRHISSERPROPROHISALA
16   VALTYRILELEUPROASPARGLYSASNGLY
17   GLYMETLYSILEGLUTYRASNLYSALAPHE
18   ASPVALMETGLYGLYGLYHISGLNMETALA
19   ARGHISALAGLNPHEASNLYSPROLEUGLY
20   ALATRPGLUGLUASPTYRPROLEUTYRHIS
21   HISLEUTHRVALTRPTHRSERPHEGLYLYS
22   ASPPROASPASPASPGLUTHRASPHISLEU
23   THRILEVALGLUVALILELYSALAVALASP
24   LEUGLUTHRTYRARG

Samples:

sample_1: gfp, [U-13C; U-15N; U-2H], 0.8 mM; Tris-HCl 20 mM; sodium chloride 10 mM; EDTA 2 mM; DSS 0.01%; H2O 90%; D2O 10%

sample_2: gfp, [U-13C; U-15N], 0.8 mM; Tris-HCl 20 mM; sodium chloride 10 mM; EDTA 2 mM; DSS 0.01%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 10 mM; pH: 7.0; pressure: 1.0 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
4D 13C,15N-edited NOESYsample_2isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

FELIX, Accelrys Software Inc. - chemical shift assignment, processing

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

PDB
GB ADI71927 ADI71928 ADI71929 ADI71930 ADI71931

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