BMRB Entry 30312

Name: Solution structure of the de novo mini protein gHEEE_02
Published: 2018-07-03

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PDB ID: 5w9f
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30312
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:

Solution structure of the de novo mini protein gHEEE_02

Deposition date:

2017-06-23

Original release date:

2018-07-03

Authors:

Szyperski, T.; Pulavarti, S.; Shaw, E.; Bahl, C.; Garry, B.; Baker, D.

Citation:

Citation: Buchko, Garry; Pulavarti, Surya; Ovchinnikov, Victor; Shaw, Elizabeth; Rettie, Stephen; Myler, Peter; Karplus, Martin; Szyperski, Thomas; Baker, David; Bahl, Christopher. "Cytosolic expression, solution structures, and molecular dynamics simulation of genetically encodable disulfide-rich de novo designed peptides" Protein Sci. 27, 1611-1623 (2018).
PubMed: 30152054

Assembly members:

Assembly members:
De novo mini protein gHEEE_02, polymer, 41 residues, 4900.680 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: 32630 Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pCDB367

Entity Sequences (FASTA):

Entity Sequences (FASTA):
De novo mini protein gHEEE_02: SQETRKKCTEMKKKFKNCEV RCDESNHCVEVRCSDTKYTL C

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	181
15N chemical shifts	46
1H chemical shifts	284

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 41 residues - 4900.680 Da.

1

SER

GLN

GLU

THR

ARG

LYS

CYS

THR

GLU

2

MET

LYS

PHE

LYS

ASN

CYS

GLU

VAL

3

ARG

CYS

ASP

GLU

SER

ASN

HIS

CYS

VAL

GLU

4

VAL

ARG

CYS

SER

ASP

THR

LYS

TYR

THR

LEU

5

CYS

Samples:

sample_1: DSS 5 uM; d20 10%; gHEEE_02, [U-13C;15N], 1 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 50 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 15N/13Caliphatic/13Caromatic-edited [1H,1H]-NOESY	sample_1	isotropic	sample_conditions_1
GFT 4,3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

CARA v1.8, Keller and Wuthrich - chemical shift assignment, chemical shift calculation

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

PROSA v6.4, Guntert - processing

PSVS v1.5, Bhattacharya and Montelione - data analysis

VNMR, Varian - collection

XEASY, Bartels et al. - data analysis

NMR spectrometers:

Varian INOVA 750 MHz

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