BMRB Entry 30241

Name: Solution structure of the de novo mini protein EEHEE_rd3_1049
Published: 2017-07-20

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PDB ID: 5up1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30241
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 EEHEE_rd3_1049

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:

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, 64 residues, 7191.284 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: MGSSHHHHHHSSGLVPRGSH MTTVKLGDIKVTFDNPEKAK KYAQKLAKIYQLTVHVHGDT IHVK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	202
15N chemical shifts	42
1H chemical shifts	328

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 64 residues - 7191.284 Da.

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

THR

VAL

LYS

LEU

GLY

ASP

ILE

LYS

4

VAL

THR

PHE

ASP

ASN

PRO

GLU

LYS

ALA

LYS

5

LYS

TYR

ALA

GLN

LYS

LEU

ALA

LYS

ILE

TYR

6

GLN

LEU

THR

VAL

HIS

VAL

HIS

GLY

ASP

THR

7

ILE

HIS

VAL

LYS

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 HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	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

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 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