BMRB Entry 34572

Name: Solution structure of the fluorogen-activating protein FAST in complex with the ligand N871b
Published: 2021-04-23

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PDB ID: 7ava
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34572
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	576
15N chemical shifts	139
1H chemical shifts	954

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1
2	unit_2	2

Entities:

Entity 1, unit_1 138 residues - 15249.174 Da.

1

MET

GLU

HIS

VAL

ALA

PHE

GLY

SER

GLU

ASP

2

ILE

GLU

ASN

THR

LEU

ALA

LYS

MET

ASP

3

GLY

GLN

LEU

ASP

GLY

LEU

ALA

PHE

GLY

ALA

4

ILE

GLN

LEU

ASP

GLY

ASP

GLY

ASN

ILE

LEU

5

GLN

TYR

ASN

ALA

GLU

GLY

ASP

ILE

THR

6

GLY

ARG

ASP

PRO

LYS

GLN

VAL

ILE

GLY

LYS

7

ASN

PHE

LYS

ASP

VAL

ALA

PRO

GLY

THR

8

ASP

SER

PRO

GLU

PHE

TYR

GLY

LYS

PHE

LYS

9

GLU

GLY

VAL

ALA

SER

GLY

ASN

LEU

ASN

THR

10

MET

PHE

GLU

TRP

MET

ILE

PRO

THR

SER

ARG

11

GLY

PRO

THR

LYS

VAL

LYS

VAL

HIS

MET

LYS

12

LYS

ALA

LEU

SER

GLY

ASP

SER

TYR

TRP

VAL

13

PHE

VAL

LYS

ARG

VAL

LYS

LEU

ALA

14

LEU

GLU

HIS

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:

Name	Sample	Sample state	Sample conditions
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_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