BMRB Entry 27420

Name: Chemical shifts for the de novo mini protein gHH_44 in the reduced state.
Published: 2018-04-11

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27420

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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:

Chemical shifts for the de novo mini protein gHH_44 in the reduced state.

Deposition date:

2018-03-06

Original release date:

2018-04-11

Authors:

Buchko, Garry; Bahl, Christopher; Baker, David

Citation:

Citation: Buchko, Garry; Pulavarti, Surya; Ovchinnikov, Victor; Shaw, Elizabeth; Rettie, Stephen; Myler, Peter; Karplus, Martin; Szyperski, Thomas; Baker, David; Bahl, Christopher. "Cytosolic expression, solution structures, and molecular dynamics simulation of genetically encodable disulfide-rich de novo designed peptides" Protein Sci. 27, 1611-1623 (2018).
PubMed: 30152054

Assembly members:

Assembly members:
gHH_44, polymer, 28 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pCDB368

Entity Sequences (FASTA):

Entity Sequences (FASTA):
gHH_44: AEDCERIRKELEKNPNDEIK KKLEKCQA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	72
15N chemical shifts	28
1H chemical shifts	163

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	gHH_44	1

Entities:

Entity 1, gHH_44 28 residues - Formula weight is not available

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: gHH_44, [U-99% 13C; U-99% 15N], 1 mM; sodium acetate 20 mM; TCEP 5 mM

sample_conditions_1: ionic strength: 25 mM; pH: 4.8; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

Felix v2007, Accelrys Software Inc. - processing

SPARKY v1.4, Goddard - data analysis

NMR spectrometers:

Agilent VXRS 800 MHz
Agilent VXRS 600 MHz

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