BMRB Entry 50907

Name: Rules for designing protein fold switches and their implications for the folding code
Published: 2023-01-03

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50907

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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: Rules for designing protein fold switches and their implications for the folding code PubMed: 36702827

Deposition date: 2021-04-22 Original release date: 2023-01-03

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

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

Assembly members:
entity_1, polymer, 56 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: pA-YRGL

Entity Sequences (FASTA):
entity_1: NPNLDQKQLAQAKELAIKAL KQYGIGVEKIKLIGNAKTVE AVEKLKQGILLVYQIE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	160
15N chemical shifts	54
1H chemical shifts	54

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	A1	1

Entities:

Entity 1, A1 56 residues - Formula weight is not available

1

ASN

PRO

ASN

LEU

ASP

GLN

LYS

GLN

LEU

ALA

2

GLN

ALA

LYS

GLU

LEU

ALA

ILE

LYS

ALA

LEU

3

LYS

GLN

TYR

GLY

ILE

GLY

VAL

GLU

LYS

ILE

4

LYS

LEU

ILE

GLY

ASN

ALA

LYS

THR

VAL

GLU

5

ALA

VAL

GLU

LYS

LEU

LYS

GLN

GLY

ILE

LEU

6

LEU

VAL

TYR

GLN

ILE

GLU

Samples:

sample_1: A1, [U-13C; U-15N], 0.3 mM; D2O 5 % v/v; potassium phosphate 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 278 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3DHNCACB	sample_1	isotropic	sample_conditions_1
3DCBCACONH	sample_1	isotropic	sample_conditions_1
3DHNCO	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.61 - data collection

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