BMRB Entry 30204

Name: Solution structure of the de novo mini protein gHH_44
Published: 2017-09-25

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PDB ID: 5tx8
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30204
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 gHH_44

Deposition date:

2016-11-15

Original release date:

2017-09-25

Authors:

Buchko, G.; Bahl, C.; Baker, D.

Citation:

Citation: Bhardwaj, Gaurav; Mulligan, Vikram Khipple; Bahl, Christopher; Gilmore, Jason; Harvey, Peta; Cheneval, Olivier; Buchko, Garry; Pulavarti, Surya; Kaas, Quentin; Eletsky, Alexander; Huang, Po-Ssu; Johnsen, William; Greisen, Per Jr; Rocklin, Gabriel; Song, Yifan; Linsky, Thomas; Watkins, Andrew; Rettie, Stephen; Xu, Xianzhong; Carter, Lauren; Bonneau, Richard; Olson, James; Coutsias, Evangelos; Correnti, Colin; Szyperski, Thomas; Craik, David; Baker, David. "Accurate de novo design of hyperstable constrained peptides" Nature 538, 329-335 (2016).
PubMed: 27626386

Assembly members:

Assembly members:
entity_1, polymer, 28 residues, 3366.862 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: AEDCERIRKELEKNPNDEIK KKLEKCQA

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	117
15N chemical shifts	29
1H chemical shifts	164

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 28 residues - 3366.862 Da.

1

ALA

GLU

ASP

CYS

GLU

ARG

ILE

ARG

LYS

GLU

2

LEU

GLU

LYS

ASN

PRO

ASN

ASP

GLU

ILE

LYS

3

LYS

LEU

GLU

LYS

CYS

GLN

ALA

Samples:

sample_1: HH2, [U-99% 13C; U-99% 15N], 1 ± 0.2 mM; sodium acetate, none, 25 ± 1 mM; sodium chloride, none, 50 ± 2 mM

sample_2: HH2, [U-99% 13C; U-99% 15N], 1 ± 0.2 mM; sodium acetate, none, 25 ± 1 mM; sodium chloride, none, 50 ± 2 mM

sample_conditions_1: ionic strength: 0.075 M; pH: 4.8; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D C(CO)NH	sample_1	anisotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	anisotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	anisotropic	sample_conditions_1
3D HNCA	sample_1	anisotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	anisotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	anisotropic	sample_conditions_1
D20 exchange	sample_2	anisotropic	sample_conditions_1

Software:

CNS v1.1, Brunger A. T. et.al. - refinement

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

Felix v2007, Accelrys Software Inc. - processing

PSVS v1.5, Bhattacharya and Montelione - chemical shift assignment

SPARKY v3.115, Goddard - data analysis

NMR spectrometers:

Varian VXRS 600 MHz
Varian VXRS 800 MHz
Varian INOVA 500 MHz

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