BMRB Entry 30242

Name: Solution structure of the de novo mini protein EHEE_rd1_0284
Published: 2017-07-20

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PDB ID: 5up5
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30242
MolProbity Validation Chart

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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 the de novo mini protein EHEE_rd1_0284 PubMed: 28706065

Deposition date: 2017-02-01 Original release date: 2017-07-20

Authors: Houliston, S.; Rocklin, G.; Lemak, A.; Carter, L.; Chidyausiku, T.; Baker, D.; Arrowsmith, C.

Citation: Rocklin, Gabriel; Chidyausiku, Tamuka; Goreshnik, Inna; Ford, Alex; Houliston, Scott; Lemak, Alexander; Carter, Lauren; Ravichandran, Rashmi; Mulligan, Vikram; Chevalier, Aaron; Arrowsmith, Cheryl; Baker, David. "Global analysis of protein folding using massively parallel design, synthesis, and testing" Science 357, 168-175 (2017).

Assembly members:
entity_1, polymer, 40 residues, 4973.368 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: TQTQEFDNEEEARKAEKELR KENRRVTVTQENGRWRVTWD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	127
15N chemical shifts	24
1H chemical shifts	204

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 40 residues - 4973.368 Da.

1	THR	GLN	THR	GLN	GLU	PHE	ASP	ASN	GLU	GLU
2	GLU	ALA	ARG	LYS	ALA	GLU	LYS	GLU	LEU	ARG
3	LYS	GLU	ASN	ARG	ARG	VAL	THR	VAL	THR	GLN
4	GLU	ASN	GLY	ARG	TRP	ARG	VAL	THR	TRP	ASP

Samples:

sample_1: protein, [U-13C; U-15N], 400 uM; sodium chloride, unlabelled, 150 mM; sodium phosphate, unlabelled, 50 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

ABACUS, Lemak and Arrowsmith - chemical shift assignment

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

SPARKY, Goddard - peak picking

NMR spectrometers:

Bruker AvanceII 800 MHz
Bruker AvanceIII 600 MHz

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

1	THR	GLN	THR	GLN	GLU	PHE	ASP	ASN	GLU	GLU
2	GLU	ALA	ARG	LYS	ALA	GLU	LYS	GLU	LEU	ARG
3	LYS	GLU	ASN	ARG	ARG	VAL	THR	VAL	THR	GLN
4	GLU	ASN	GLY	ARG	TRP	ARG	VAL	THR	TRP	ASP

1	THR	GLN	THR	GLN	GLU	PHE	ASP	ASN	GLU	GLU
2	GLU	ALA	ARG	LYS	ALA	GLU	LYS	GLU	LEU	ARG
3	LYS	GLU	ASN	ARG	ARG	VAL	THR	VAL	THR	GLN
4	GLU	ASN	GLY	ARG	TRP	ARG	VAL	THR	TRP	ASP

1	THR	GLN	THR	GLN	GLU	PHE	ASP	ASN	GLU	GLU
2	GLU	ALA	ARG	LYS	ALA	GLU	LYS	GLU	LEU	ARG
3	LYS	GLU	ASN	ARG	ARG	VAL	THR	VAL	THR	GLN
4	GLU	ASN	GLY	ARG	TRP	ARG	VAL	THR	TRP	ASP