BMRB Entry 30240

Name: Solution structure of the de novo mini protein HHH_rd1_0142
Published: 2017-07-20

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PDB ID: 5uoi
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30240
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 HHH_rd1_0142

Deposition date:

2017-01-31

Original release date:

2017-07-20

Authors:

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

Citation:

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).
PubMed: 28706065

Assembly members:

Assembly members:
entity_1, polymer, 43 residues, 5190.805 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: RKWEEIAERLREEFNINPEE AREAVEKAGGNEEEARRIVK KRL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	168
15N chemical shifts	40
1H chemical shifts	280

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 43 residues - 5190.805 Da.

1

ARG

LYS

TRP

GLU

ILE

ALA

GLU

ARG

LEU

2

ARG

GLU

PHE

ASN

ILE

ASN

PRO

GLU

3

ALA

ARG

GLU

ALA

VAL

GLU

LYS

ALA

GLY

4

ASN

GLU

ALA

ARG

ILE

VAL

LYS

5

LYS

ARG

LEU

Samples:

sample_1: protein, [U-13C; U-15N], 400 ± 200 uM; sodium chloride, unlabeled, 150 mM; sodium phosphate, unlabeled, 50 mM

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

Experiments:

Name	Sample	Sample state	Sample conditions
3D 15N NOESY	sample_1	isotropic	sample_conditions_1
3D HNCA	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 HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 13C NOESY (aromatic and aliphatic)	sample_1	isotropic	sample_conditions_1

Software:

ABACUS, Lemak and Arrowsmith - chemical shift assignment, peak picking

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMR spectrometers:

Bruker Avance III 600 MHz
Bruker Avance II 800 MHz

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