BMRB Entry 51719

Name: Design and characterization of a protein fold switching network
Published: 2023-01-03

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51719

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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: Design and characterization of a protein fold switching network PubMed: 36702827

Deposition date: 2022-12-02 Original release date: 2023-01-03

Authors: Ruan, Biao; He, Yanan; Chen, Yingwei; Choi, Eun Jung; Chen, Yihong; Motabar, Dana; Solomon, Tsega; Simmerman, Richard; Kauffman, Thomas; Gallagher, D. Travis; Orban, John; Bryan, Philip N.

Citation: Ruan, Biao; He, Yanan; Chen, Yingwei; Choi, Eun Jung; Chen, Yihong; Motabar, Dana; Solomon, Tsega; Simmerman, Richard; Kauffman, Thomas; Gallagher, D. Travis; Orban, John; Bryan, Philip N.. "Design and characterization of a protein fold switching network" Nat. Commun. 14, 431-431 (2023).

Assembly members:
entity_1, polymer, 87 residues, Formula weight is not available

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pH720

Entity Sequences (FASTA):
entity_1: TTYKLILNLKFAFGDTNSEA VDAAEAEKKFKQYANDHGVD GEWTYDDATKTFTVTAKDSH ADRVRELAQRLRQRPRVERV EITEVTE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	231
15N chemical shifts	68
1H chemical shifts	134

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Sb4	1

Entities:

Entity 1, Sb4 87 residues - Formula weight is not available

1

THR

TYR

LYS

LEU

ILE

LEU

ASN

LEU

LYS

2

PHE

ALA

PHE

GLY

ASP

THR

ASN

SER

GLU

ALA

3

VAL

ASP

ALA

GLU

ALA

GLU

LYS

PHE

4

LYS

GLN

TYR

ALA

ASN

ASP

HIS

GLY

VAL

ASP

5

GLY

GLU

TRP

THR

TYR

ASP

ALA

THR

LYS

6

THR

PHE

THR

VAL

THR

ALA

LYS

ASP

SER

HIS

7

ALA

ASP

ARG

VAL

ARG

GLU

LEU

ALA

GLN

ARG

8

LEU

ARG

GLN

ARG

PRO

ARG

VAL

GLU

ARG

VAL

9

GLU

ILE

THR

GLU

VAL

THR

GLU

Samples:

sample_1: Sb4, [U-13C; U-15N], 0.3 mM; potassium phosphate 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.6 - data collection

NMRFAM-SPARKY - chemical shift assignment

NMRPipe - data processing

NMR spectrometers:

Bruker Avance 600 MHz

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