BMRB Entry 34572

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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/BMR34572
MolProbity Validation Chart

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Title:
Solution structure of the fluorogen-activating protein FAST in complex with the ligand N871b
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.
entity_S1Q, non-polymer, 335.357 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 shifts576
15N chemical shifts139
1H chemical shifts954

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_22

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

Entity 2, unit_2 - C19 H17 N3 O3 - 335.357 Da.

1   S1Q

Samples:

sample_1: FAST, [U-13C; U-15N], 0.85 ± 0.05 mM; N87 0.90 ± 0.01 mM; sodium phosphate 20 mM; sodium chloride 20 mM; sodium azide 0.01%

sample_conditions_1: ionic strength: 40 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1

Software:

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

CARA, Keller and Wuthrich - chemical shift assignment

qMDD, Orekhov, Mayzel - processing

TALOS-N, Cornilescu, Bax - data analysis

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

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