BMRB Entry 50910

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/BMR50910

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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

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:

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).
PubMed: 36702827

Assembly members:

Assembly members:
entity_1, polymer, 56 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pA-YRGL

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: ATFKLVLNGKTLKGETTTEA VDAATALKNFGAYAQDVGVD GAWTYDDATKTFTVGE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	161
15N chemical shifts	55
1H chemical shifts	116

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	B1	1

Entities:

Entity 1, B1 56 residues - Formula weight is not available

1

ALA

THR

PHE

LYS

LEU

VAL

LEU

ASN

GLY

LYS

2

THR

LEU

LYS

GLY

GLU

THR

GLU

ALA

3

VAL

ASP

ALA

THR

ALA

LEU

LYS

ASN

PHE

4

GLY

ALA

TYR

ALA

GLN

ASP

VAL

GLY

VAL

ASP

5

GLY

ALA

TRP

THR

TYR

ASP

ALA

THR

LYS

6

THR

PHE

THR

VAL

GLY

GLU

Samples:

sample_1: B1, [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: 298 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
3DHNHA	sample_1	isotropic	sample_conditions_1
3DHNCO	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.61 - collection

NMRFAM-SPARKY - data analysis

NMR spectrometers:

Bruker Avance 600 MHz

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