BMRB Entry 31033

Name: Solution structure of a model HEEH mini-protein (HEEH_TK_rd5_0958)
Published: 2022-09-27

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PDB ID: 8doa
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31033
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution structure of a model HEEH mini-protein (HEEH_TK_rd5_0958) PubMed: 36191185

Deposition date: 2022-07-12 Original release date: 2022-09-27

Authors: Houliston, S.; Kim, T.-E., T.; Rocklin, G.; Arrowsmith, C.

Citation: Kim, Tae-Eun; Tsuboyama, Kotaro; Houliston, Scott; Martell, Cydney; Phoumyvong, Claire; Lemak, Alexander; Haddox, Hugh; Arrowsmith, Cheryl; Rocklin, Gabriel. "Dissecting the stability determinants of a challenging de novo protein fold using massively parallel design and experimentation" Proc. Natl. Acad. Sci. U. S. A. 119, e2122676119-e2122676119 (2022).

Assembly members:
entity_1, polymer, 64 residues, 7449.431 Da.

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

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH MDIEEIEKKARKILEKGDSI EIAGFEVRDEEDLKKILEWL RRHG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1
- spectral_peak_list_2

Data type	Count
13C chemical shifts	193
15N chemical shifts	43
1H chemical shifts	316

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 64 residues - 7449.431 Da.

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

ASP

ILE

GLU

ILE

GLU

LYS

ALA

4

ARG

LYS

ILE

LEU

GLU

LYS

GLY

ASP

SER

ILE

5

GLU

ILE

ALA

GLY

PHE

GLU

VAL

ARG

ASP

GLU

6

GLU

ASP

LEU

LYS

ILE

LEU

GLU

TRP

LEU

7

ARG

HIS

GLY

Samples:

sample_1: sodium phosphate 50 mM; sodium chloride 150 mM; protein 0.5 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 atm; temperature: 288 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

ABACUS, Lemak and Arrowsmith - chemical shift assignment

Sparky, Goddard - peak picking

NMR spectrometers:

Bruker AVANCE III 600 MHz

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