BMRB Entry 34746

Name: Solution structure of nanoFAST/HBR-DOM2 complex
Published: 2022-11-28

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PDB ID: 8ao0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34746
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution structure of nanoFAST/HBR-DOM2 complex PubMed: 36232662

Deposition date: 2022-08-08 Original release date: 2022-11-28

Authors: Lushpa, V.; Goncharuk, M.; Goncharuk, S.; Baleeva, N.; Baranov, M.; Mineev, K.

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).

Assembly members:
entity_1, polymer, 112 residues, 12489.214 Da.
entity_O1F, non-polymer, 297.350 Da.

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

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

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

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	472
15N chemical shifts	110
1H chemical shifts	776

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_1 112 residues - 12489.214 Da.

1

MET

PHE

GLY

ALA

ILE

GLN

LEU

ASP

GLY

ASP

2

GLY

ASN

ILE

LEU

GLN

TYR

ASN

ALA

GGL

3

GLY

ASP

ILE

THR

GLY

ARG

ASP

PRO

LYS

GLN

4

VAL

ILE

GLY

LYS

ASN

PHE

LYS

ASP

VAL

5

ALA

PRO

GLY

THR

ASP

SER

PRO

GLU

PHE

TYR

6

GLY

LYS

PHE

LYS

GLU

GLY

VAL

ALA

SER

GLY

7

ASN

LEU

ASN

THR

MET

PHE

GLU

TRP

MET

ILE

8

PRO

THR

SER

ARG

GLY

PRO

THR

LYS

VAL

LYS

9

VAL

HIS

MET

LYS

ALA

LEU

SER

GLY

ASP

10

SER

TYR

TRP

VAL

PHE

VAL

LYS

ARG

VAL

LYS

11

LEU

ALA

LEU

GLU

HIS

12

HIS

Entity 2, unit_2 - 297.350 Da.

1

O1F

Samples:

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

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

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
hbCBcarHar	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

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

TopSpin v3.0, Bruker Biospin - processing

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

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

NMR spectrometers:

Bruker AVANCE III 800 MHz

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