BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 27420

Title: Chemical shifts for the de novo mini protein gHH_44 in the reduced state.   PubMed: 30152054

Authors: Buchko, Garry; Bahl, Christopher; Baker, David

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).

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

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

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

Entity Sequences (FASTA):
gHH_44: AEDCERIRKELEKNPNDEIK KKLEKCQA

Data sets:
Data typeCount
13C chemical shifts72
15N chemical shifts28
1H chemical shifts163

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1gHH_441

Entities:

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

1   ALAGLUASPCYSGLUARGILEARGLYSGLU
2   LEUGLULYSASNPROASNASPGLUILELYS
3   LYSLYSLEUGLULYSCYSGLNALA

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_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

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