BMRB Entry 30069

Name: Solution structure of the de novo miniprotein EEHE_02
Published: 2016-09-22

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PDB ID: 5ji4
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR30069
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 miniprotein EEHE_02 PubMed: 27626386

Deposition date: 2016-04-21 Original release date: 2016-09-22

Authors: Buchko, G.; Bahl, C.

Citation: Bhardwaj, G.; Mulligan, V.; Bahl, C.; Gilmore, J.; Harvey, P.; Cheneval, O.; Buchko, G.; Pulavarti, S.; Kaas, Q.; Eletsky, A.; Huang, P.; Johnsen, W.; Greisen, P.; Rocklin, G.; Song, Y.; Linsky, T.; Watkins, A.; Rettie, S.; Xu, X.; Carter, L.; Bonneau, R.; Olson, J.; Coutsias, E.; Correnti, C.; Szyperski, T.; Craik, D.; Baker, D.. "Accurate de novo design of hyperstable constrained peptides." Nature 538, 329-335 (2016).

Assembly members:
W37, polymer, 37 residues, 4054.548 Da.

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

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

Entity Sequences (FASTA):
W37: APCECDVNGETYTVSSSEEC ERLCRKLGVTNCRVHCG

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	84
15N chemical shifts	39
1H chemical shifts	220

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 37 residues - 4054.548 Da.

1

ALA

PRO

CYS

GLU

CYS

ASP

VAL

ASN

GLY

GLU

2

THR

TYR

THR

VAL

SER

GLU

CYS

3

GLU

ARG

LEU

CYS

ARG

LYS

LEU

GLY

VAL

THR

4

ASN

CYS

ARG

VAL

HIS

CYS

GLY

Samples:

sample_1: W37, [U-99% 15N], 1 ± 0.2 mM; sodium acetate 25 ± 1 mM; sodium chloride 50 ± 1 mM; H2O 93%; D2O 7%

sample_2: W37, [U-99% 15N], 1 mM; sodium acetate 25 ± 1 mM; sodium chloride 50 ± 1 mM; D2O 100%

sample_conditions_1: ionic strength: 75 mM; pH: 4.8; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
Deuterium Exchange	sample_2	isotropic	sample_conditions_1

Software:

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

Felix v2007, Accelrys Software Inc. - processing

PSVS v1.5, Bhattacharya and Montelione - data analysis

SPARKY v3.115, Goddard - data analysis, peak picking

NMR spectrometers:

Varian INOVA 500 MHz
Varian INOVA 750 MHz

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