BMRB Entry 51338

Name: Chemical shift assignment of Sa1_V90T at 5 degrees Celsius
Published: 2023-01-04

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51338

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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: Chemical shift assignment of Sa1_V90T at 5 degrees Celsius PubMed: 36669114

Deposition date: 2022-02-22 Original release date: 2023-01-04

Authors: Solomon, Tsega; He, Yanan; Orban, John

Citation: Solomon, Tsega; He, Yanan; Sari, Nese; Chen, Yihong; Gallagher, D Travis; Bryan, Philip; Orban, John. "Reversible switching between two common protein folds in a designed system using only temperature" Proc. Natl. Acad. Sci. U. S. A. 120, e2215418120-e2215418120 (2023).

Assembly members:
entity_1, polymer, 95 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: pH0720

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

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	251
15N chemical shifts	87
1H chemical shifts	127

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Sa1 V90T	1

Entities:

Entity 1, Sa1 V90T 95 residues - Formula weight is not available

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

THR

10

THR

TYR

ALA

ASP

Samples:

sample_1: Sa1 V90T, [U-13C; U-15N], 250 uM; potassium phosphate 100 mM

sample_2: Sa1 V90T, [U-13C; U-15N], 250 uM; potassium phosphate 100 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7.0; pressure: 1 atm; temperature: 278 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D HN(CA)NNH	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

CS-Rosetta v3.2 - structure solution

NMR spectrometers:

Bruker AVANCE III 600 MHz
Bruker AVANCE III 900 MHz

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