BMRB Entry 30901

Name: Rules for designing protein fold switches and their implications for the folding code
Published: 2022-05-09

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PDB ID: 7mn1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30901
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:

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

Deposition date:

2021-04-30

Original release date:

2022-05-09

Authors:

He, Y.; Chen, Y.; Ruan, B.; Choi, J.; Chen, Y.; Motabar, D.; Solomon, T.; Simmerman, R.; Kauffman, T.; Gallagher, T.; Bryan, P.; Orban, J.

Citation:

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).
PubMed: 36702827

Assembly members:

Assembly members:
entity_1, polymer, 95 residues, 10600.333 Da.

Natural source:

Natural source: Common Name: Thermus thermophilus Taxonomy ID: 274 Superkingdom: Bacteria Kingdom: not available Genus/species: Thermus thermophilus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SKTFEVNIVLNPNLDQKQLA QAKELAIKALKQYGIGVEKI KLIGNAKTVEAVEKLKQGIL LVYQIEAPADRVNDLARELR ILDAVRRVEVTYAAD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	279
15N chemical shifts	82
1H chemical shifts	289

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 95 residues - 10600.333 Da.

1

SER

LYS

THR

PHE

GLU

VAL

ASN

ILE

VAL

LEU

2

ASN

PRO

ASN

LEU

ASP

GLN

LYS

GLN

LEU

ALA

3

GLN

ALA

LYS

GLU

LEU

ALA

ILE

LYS

ALA

LEU

4

LYS

GLN

TYR

GLY

ILE

GLY

VAL

GLU

LYS

ILE

5

LYS

LEU

ILE

GLY

ASN

ALA

LYS

THR

VAL

GLU

6

ALA

VAL

GLU

LYS

LEU

LYS

GLN

GLY

ILE

LEU

7

LEU

VAL

TYR

GLN

ILE

GLU

ALA

PRO

ALA

ASP

8

ARG

VAL

ASN

ASP

LEU

ALA

ARG

GLU

LEU

ARG

9

ILE

LEU

ASP

ALA

VAL

ARG

VAL

GLU

VAL

10

THR

TYR

ALA

ASP

Samples:

sample_1: Sa1, U-15N13C, 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 HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

CS-ROSETTA v3.2, Shen, Vernon, Baker and Bax - refinement

TopSpin, Bruker Biospin - collection

NMRFAM-SPARKY, Lee W, Tonelli M, Markley JL - chemical shift assignment, data analysis

CS-ROSETTA, Shen, Vernon, Baker and Bax - structure calculation

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

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