BMRB Entry 34573

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34573
MolProbity Validation Chart

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Title:
Solution structure of the fluorogen-activating protein FAST in the apo state
Deposition date:
2020-11-05
Original release date:
2021-04-23
Authors:
Mineev, K.; Goncharuk, S.; Baranov, M.
Citation:

Citation: Mineev, K.; Goncharuk, S.; Goncharuk, M.; Povarova, N.; Sokolov, A.; Baleeva, N.; Smirnov, A.; Myasnyanko, I.; Ruchkin, D.; Bukhdruker, S.; Remeeva, A.; Mishin, A.; Borshchevskiy, V.; Gordeliy, V.; Arseniev, A.; Gorbachev, D.; Gavrikov, A.; Mishin, A.; Baranov, M.. "NanoFAST: structure-based design of a small fluorogen-activating protein with only 98 amino acids"  Chem. Sci. 12, 6719-6725 (2021).
PubMed: 34040747

Assembly members:

Assembly members:
entity_1, polymer, 138 residues, 15249.174 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: 32630   Superkingdom: not available   Kingdom: not available   Genus/species: synthetic construct

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MEHVAFGSEDIENTLAKMDD GQLDGLAFGAIQLDGDGNIL QYNAAEGDITGRDPKQVIGK NFFKDVAPGTDSPEFYGKFK EGVASGNLNTMFEWMIPTSR GPTKVKVHMKKALSGDSYWV FVKRVKLAAALEHHHHHH

Data sets:
Data typeCount
13C chemical shifts552
15N chemical shifts118
1H chemical shifts904

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 138 residues - 15249.174 Da.

1   METGLUHISVALALAPHEGLYSERGLUASP
2   ILEGLUASNTHRLEUALALYSMETASPASP
3   GLYGLNLEUASPGLYLEUALAPHEGLYALA
4   ILEGLNLEUASPGLYASPGLYASNILELEU
5   GLNTYRASNALAALAGLUGLYASPILETHR
6   GLYARGASPPROLYSGLNVALILEGLYLYS
7   ASNPHEPHELYSASPVALALAPROGLYTHR
8   ASPSERPROGLUPHETYRGLYLYSPHELYS
9   GLUGLYVALALASERGLYASNLEUASNTHR
10   METPHEGLUTRPMETILEPROTHRSERARG
11   GLYPROTHRLYSVALLYSVALHISMETLYS
12   LYSALALEUSERGLYASPSERTYRTRPVAL
13   PHEVALLYSARGVALLYSLEUALAALAALA
14   LEUGLUHISHISHISHISHISHIS

Samples:

sample_1: FAST, [U-13C; U-15N], 1 ± 0.1 mM; sodium phosphate 20 ± 0.1 mM; sodium chloride 20 ± 0.1 mM; sodium azide 0.1%

sample_2: FAST, [U-13C; U-15N], 1 ± 0.1 mM; sodium phosphate 20 ± 0.1 mM; sodium chloride 20 ± 0.1 mM; sodium azide 0.1%

sample_conditions_1: ionic strength: 40 mM; pH: 7.0; pressure: 1 atm; temperature: 318 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1

Software:

CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - structure calculation

CARA v3.98.13, Keller and Wuthrich - chemical shift assignment

TopSpin, Bruker Biospin - processing

TALOS-N, Bax - data analysis

qMDD, Orekhov, Mayzel - processing

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

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