BMRB Entry 34032

Name: Engineering protein stability with atomic precision in a monomeric miniprotein
Published: 2017-05-12

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PDB ID: 5lo3
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34032
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:

Engineering protein stability with atomic precision in a monomeric miniprotein

Deposition date:

2016-08-08

Original release date:

2017-05-12

Authors:

Baker, E.; Hudson, K.; Williams, C.; Bartlett, G.; Heal, J.; Sessions, R.; Crump, M.; Woolfson, D.

Citation:

Citation: Baker, E.; Williams, C.; Hudson, K.; Bartlett, G.; Heal, J.; Porter Goff, K.; Sessions, R.; Crump, M.; Woolfson, D.. "Engineering protein stability with atomic precision in a monomeric miniprotein" Nat. Chem. Biol. 13, 764-770 (2017).
PubMed: 28530710

Assembly members:

Assembly members:
entity_1, polymer, 36 residues, 3849.365 Da.

Natural source:

Natural source: Common Name: Streptococcus mutans Taxonomy ID: 1309 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptococcus mutans

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: XPPTKPTKPGDNATPEKLAK XQADLAKXQKDLADXX

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	39
15N chemical shifts	32
1H chemical shifts	227

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 36 residues - 3849.365 Da.

1

ACE

PRO

THR

LYS

PRO

THR

LYS

PRO

GLY

2

ASP

ASN

ALA

THR

PRO

GLU

LYS

LEU

ALA

LYS

3

0A1

GLN

ALA

ASP

LEU

ALA

LYS

0A1

GLN

LYS

4

ASP

LEU

ALA

ASP

0A1

NH2

Samples:

sample_1: KH2PO4 1.8 mM; Na2HPO4 8.2 mM; NaCl 137 mM; NaOH 13.7 mM; PPalpha_OMe 1 mM

sample_conditions_1: ionic strength: 0.1698 M; pH: 7.4; pressure: 1 atm; temperature: 278 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D DQF-COSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - refinement

Analysis, CCPN - chemical shift assignment, peak picking

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Bruker AvanceIII 700 MHz
Bruker AvanceIII 900 MHz

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