BMRB Entry 30777

Title:
Solution structure of a reconstructed XCL1 ancestor
Deposition date:
2020-07-20
Original release date:
2020-12-26
Authors:
Tyler, R.; Peterson, F.; Volkman, B.
Citation:

Citation: Dishman, A.; Tyler, R.; Fox, J.; Kleist, A.; Prehoda, K.; Babu, M.; Peterson, F.; Volkman, B.. "Evolution of fold switching in a metamorphic protein"  Science 371, 86-90 (2021).
PubMed: 33384377

Assembly members:

Assembly members:
entity_1, polymer, 64 residues, 7483.078 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: 32644   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: pET28

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts289
15N chemical shifts64
1H chemical shifts418

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 64 residues - 7483.078 Da.

1   ALAARGLYSSERCYSCYSLEULYSTYRTHR
2   LYSARGPROLEUPROLEULYSARGILELYS
3   SERTYRTHRILEGLNSERASNGLUALACYS
4   ASNILELYSALAILEILEPHETHRTHRLYS
5   LYSGLYARGLYSILECYSALAASNPROASN
6   GLULYSTRPVALGLNLYSALAMETLYSHIS
7   LEUASPLYSLYS

Samples:

sample_1: Anc.0, [U-99% 13C; U-99% 15N], 1.0 mM; sodium phosphate 20 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 29 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

TopSpin v3, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

XEASY, Bartels et al. - data analysis, peak picking

GARANT, Bartels, Guntert, Billeter and Wuthrich - chemical shift assignment

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

TALOS, Cornilescu, Delaglio and Bax - data analysis

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - geometry optimization

NMR spectrometers:

  • Bruker AVANCE DRX 600.13 MHz

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