BMRB Entry 34613

Name: Solution structure of Boskar4; a de novo designed G-CSF agonist
Published: 2021-10-01

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PDB ID: 7ny0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34613
MolProbity Validation Chart

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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 Boskar4; a de novo designed G-CSF agonist PubMed: 35618709

Deposition date: 2021-03-19 Original release date: 2021-10-01

Authors: ElGamacy, M.; Coles, M.

Citation: Skokowa, Julia; Alvarez, Birte; Coles, Murray; Ritter, Malte; Nasri, Masoud; Haaf, Jeremy; Aghaallaei, Narges; Xu, Yun; Mir, Perihan; Krahl, Ann-Christin; Rogers, Katherine; Maksymenko, Kateryna; Bajoghli, Baubak; Welte, Karl; Lupas, Andrei; Muller, Patrick; ElGamacy, Mohammad. "A topological refactoring design strategy yields highly stable granulopoietic proteins" Nat. Commun. 13, 2948-2948 (2022).

Assembly members:
entity_1, polymer, 121 residues, 13014.956 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: LAAALAEIYKGLAEYQARLK SLEGISPELGPALDALRLDM ADFATTMAQAMEEGLDSLPQ SFLLKALEQIRKIQADAAAL REKLAATYKGNDRAAAAVEI AAQLEAFLEKAYQILRHLAA A

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	495
15N chemical shifts	115
1H chemical shifts	791

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 121 residues - 13014.956 Da.

1

LEU

ALA

LEU

ALA

GLU

ILE

TYR

LYS

2

GLY

LEU

ALA

GLU

TYR

GLN

ALA

ARG

LEU

LYS

3

SER

LEU

GLU

GLY

ILE

SER

PRO

GLU

LEU

GLY

4

PRO

ALA

LEU

ASP

ALA

LEU

ARG

LEU

ASP

MET

5

ALA

ASP

PHE

ALA

THR

MET

ALA

GLN

ALA

6

MET

GLU

GLY

LEU

ASP

SER

LEU

PRO

GLN

7

SER

PHE

LEU

LYS

ALA

LEU

GLU

GLN

ILE

8

ARG

LYS

ILE

GLN

ALA

ASP

ALA

LEU

9

ARG

GLU

LYS

LEU

ALA

THR

TYR

LYS

GLY

10

ASN

ASP

ARG

ALA

VAL

GLU

ILE

11

ALA

GLN

LEU

GLU

ALA

PHE

LEU

GLU

LYS

12

ALA

TYR

GLN

ILE

LEU

ARG

HIS

LEU

ALA

13

ALA

Samples:

sample_1: Boskar4, [U-100% 15N], 500 uM; sodium phosphate 150 mM

sample_2: Boskar4, [U-100% 13C; U-100% 15N], 500 uM; sodium phosphate 150 mM

sample_conditions_1: ionic strength: 450 mM; pH: 7.5; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D C(CCO)NH	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D-CNH-NOESY	sample_2	isotropic	sample_conditions_1
13C-HSQC-NOESY	sample_2	isotropic	sample_conditions_1
2D-NOESY	sample_1	isotropic	sample_conditions_1

Software:

TopSpin, Bruker Biospin - collection

Sparky, Goddard - chemical shift assignment

CoMAND, ElGamacy, Riss, Zhu, Truffault, Murray, Coles - structure calculation

NMR spectrometers:

Bruker AVANCE III 600 MHz
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