BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 27230

Title: Elastin-like Protein 40 (ELP40)   PubMed: 29642027

Deposition date: 2017-08-22 Original release date: 2018-04-18

Authors: Zhang, Yue; Fitzkee, Nicholas

Citation: Zhang, Yue; Zai-Rose, Valeria; Price, Cody; Ezzell, Nicholas; Bidwell, Gene; Correia, John; Fitzkee, Nicholas. "Modeling the Early Stages of Phase Separation in Disordered Elastin-like Proteins."  Biophys. J. 114, 1563-1578 (2018).

Assembly members:
Elastin-like_Protein_40_(ELP40), polymer, 207 residues, Formula weight is not available

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: purified from the natural source   Host organism: Escherichia coli

Entity Sequences (FASTA):
Elastin-like_Protein_40_(ELP40): VPGKGVPGVGVPGVGVPGVG VPGVGVPGVGVPGVGVPGVG VPGTGVPGVGVPGVGVPGVG VPGVGVPGVGVPGVGVPGVG VPGAGVPGVGVPGVGVPGVG VPGVGVPGVGVPGVGVPGVG VPGIGVPGVGVPGVGVPGVG VPGVGVPGVGVPGVGVPGVG VPGSGVPGVGVPGVGVPGVG VPGVGVPGVGVPGVGVPGVG VPGLGWP

Data typeCount
13C chemical shifts1236
15N chemical shifts414
1H chemical shifts1420

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1ELP40, trans conformer1
2ELP40, cis conformer1

Entities:

Entity 1, ELP40, trans conformer 207 residues - Formula weight is not available

This is a elastin-like protein, which has 41 repeats.

1   VALPROGLYLYSGLYVALPROGLYVALGLY
2   VALPROGLYVALGLYVALPROGLYVALGLY
3   VALPROGLYVALGLYVALPROGLYVALGLY
4   VALPROGLYVALGLYVALPROGLYVALGLY
5   VALPROGLYTHRGLYVALPROGLYVALGLY
6   VALPROGLYVALGLYVALPROGLYVALGLY
7   VALPROGLYVALGLYVALPROGLYVALGLY
8   VALPROGLYVALGLYVALPROGLYVALGLY
9   VALPROGLYALAGLYVALPROGLYVALGLY
10   VALPROGLYVALGLYVALPROGLYVALGLY
11   VALPROGLYVALGLYVALPROGLYVALGLY
12   VALPROGLYVALGLYVALPROGLYVALGLY
13   VALPROGLYILEGLYVALPROGLYVALGLY
14   VALPROGLYVALGLYVALPROGLYVALGLY
15   VALPROGLYVALGLYVALPROGLYVALGLY
16   VALPROGLYVALGLYVALPROGLYVALGLY
17   VALPROGLYSERGLYVALPROGLYVALGLY
18   VALPROGLYVALGLYVALPROGLYVALGLY
19   VALPROGLYVALGLYVALPROGLYVALGLY
20   VALPROGLYVALGLYVALPROGLYVALGLY
21   VALPROGLYLEUGLYTRPPRO

Samples:

sample_1: ELP40, [U-100% 13C; U-100% 15N], 1 mM; sodium acetate 50 mM; DSS 200 uM; D2O 6%

sample_conditions_1: pH: 4.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D (HACA)CONsample_1isotropicsample_conditions_1
3D (HACA)N(CA)CONsample_1isotropicsample_conditions_1

Software:

SPARKY v3.113, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts