BMRB Entry 34747

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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/BMR34747
MolProbity Validation Chart

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Title:
solution structure of nanoFAST fluorogen-activating protein in the apo state
Deposition date:
2022-08-08
Original release date:
2022-11-28
Authors:
Lushpa, V.; Goncharuk, M.; Goncharuk, S.; Baranov, M.; Mineev, K.
Citation:

Citation: Lushpa, V.; Baleeva, N.; Goncharuk, S.; Goncharuk, M.; Arseniev, A.; Baranov, M.; Mineev, K.. "Spatial Structure of NanoFAST in the Apo State and in Complex with its Fluorogen HBR-DOM2."  Int. J. Mol. Sci. 23, 11361-11361 (2022).
PubMed: 36232662

Assembly members:

Assembly members:
entity_1, polymer, 112 residues, 12489.214 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MFGAIQLDGDGNILQYNAAE GDITGRDPKQVIGKNFFKDV APGTDSPEFYGKFKEGVASG NLNTMFEWMIPTSRGPTKVK VHMKKALSGDSYWVFVKRVK LAAALEHHHHHH

Data sets:
Data typeCount
13C chemical shifts467
15N chemical shifts111
1H chemical shifts751

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 112 residues - 12489.214 Da.

1   METPHEGLYALAILEGLNLEUASPGLYASP
2   GLYASNILELEUGLNTYRASNALAALAGLU
3   GLYASPILETHRGLYARGASPPROLYSGLN
4   VALILEGLYLYSASNPHEPHELYSASPVAL
5   ALAPROGLYTHRASPSERPROGLUPHETYR
6   GLYLYSPHELYSGLUGLYVALALASERGLY
7   ASNLEUASNTHRMETPHEGLUTRPMETILE
8   PROTHRSERARGGLYPROTHRLYSVALLYS
9   VALHISMETLYSLYSALALEUSERGLYASP
10   SERTYRTRPVALPHEVALLYSARGVALLYS
11   LEUALAALAALALEUGLUHISHISHISHIS
12   HISHIS

Samples:

sample_1: NaPi 20 mM; NaCl 20 mM; sodium azide 0.001%

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
hbCBcarHarsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

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

TopSpin v3.0, Bruker Biospin - processing

qMDD v3.2, Maxim Mayzel, Krzysztof Kazimierczuk, Vladislav Orekhov - processing

CARA v1.9.1.7, Keller and Wuthrich - chemical shift assignment, peak picking

MOLMOL, Koradi, Billeter and Wuthrich - 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