BMRB Entry 34295

Name: Stabilising and Understanding a Miniprotein by Rational Design.
Published: 2019-07-02

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PDB ID: 6gwx
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34295
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:

Stabilising and Understanding a Miniprotein by Rational Design.

Deposition date:

2018-06-26

Original release date:

2019-07-02

Authors:

Porter Goff, K.; Williams, C.; Baker, E.; Nicol, D.; Samphire, J.; Zieleniewski, F.; Crump, M.; Woolfson, D.

Citation:

Citation: Porter Goff, K.; Nicol, D.; Williams, C.; Crump, M.; Zieleniewski, F.; Samphire, J.; Baker, E.; Woolfson, D.. "Stabilizing and Understanding a Miniprotein by Rational Redesign." Biochemistry 58, 3060-3064 (2019).
PubMed: 31251570

Assembly members:

Assembly members:
entity_1, polymer, 36 residues, 3791.348 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: XPPKKPKKPGDNATPEKLAA YEKELAAYEKELAAYX

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	35
15N chemical shifts	30
1H chemical shifts	241

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 - 3791.348 Da.

1

ACE

PRO

LYS

PRO

LYS

PRO

GLY

2

ASP

ASN

ALA

THR

PRO

GLU

LYS

LEU

ALA

3

TYR

GLU

LYS

GLU

LEU

ALA

TYR

GLU

LYS

4

GLU

LEU

ALA

TYR

NH2

Samples:

sample_1: Optimised PPa-TYR 1 ± 0.1 mM; Na2HPO4 8.2 ± 0.1 mM; KH2PO4 1.8 ± 0.1 mM; KCL 2.7 ± 0.1 mM; NaCl 137 ± 0.1 mM; D2O, [U-99% 2H], 10 ± 0.1 %

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 100ms NOESY	sample_1	isotropic	sample_conditions_1
2D 100ms NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H 250ms NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H 250ms NOESY	sample_1	isotropic	sample_conditions_1
1H-13N HSQC	sample_1	isotropic	sample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

ARIA v2.3.1, Linge, O'Donoghue and Nilges - structure calculation

CcpNmr Analysis v2.4.1, CCPN - chemical shift assignment, peak picking

TopSpin v3.5, Bruker Biospin - collection

VNMR v4, Varian - collection

NMRDraw v9.5, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRPipe v9.5, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Bruker AvanceIII 700 MHz
Varian VNMRS 600 MHz

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