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 30527

Title: De novo Designed Protein Foldit3   PubMed: 31168091

Authors: Liu, G.; Ishida, Y.; Swapna, G.; Kleinfelter, S.; Koepnick, B.; Baker, D.; Montelione, G.

Citation: Koepnick, Brian; Flatten, Jeff; Husain, Tamir; Ford, Alex; Silva, Daniel-Adriano; Bick, Matthew; Bauer, Aaron; Liu, Gaohua; Ishida, Yojiro; Boykov, Alexander; Estep, Roger; Kleinfelter, Susan; Norgard-Solano, Toke; Wei, Linda; Players, Foldit; Montelione, Gaetano; DiMaio, Frank; Popovic, Zoran; Khatib, Firas; Cooper, Seth; Baker, David. "De novo protein design by citizen scientists."  Nature 570, 390-394 (2019).

Assembly members:
entity_1, polymer, 97 residues, 11725.060 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli K-12

Entity Sequences (FASTA):
entity_1: MGHHHHHHENLYFQSHMTDE LLERLRQLFEELHERGTEIV VEVHINGERDEIRVRNISKE ELKKLLERIREKIEREGSSE VEVNVHSGGQTWTFNEK

Data sets:
Data typeCount
13C chemical shifts285
15N chemical shifts92
1H chemical shifts605

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 97 residues - 11725.060 Da.

1   METGLYHISHISHISHISHISHISGLUASN
2   LEUTYRPHEGLNSERHISMETTHRASPGLU
3   LEULEUGLUARGLEUARGGLNLEUPHEGLU
4   GLULEUHISGLUARGGLYTHRGLUILEVAL
5   VALGLUVALHISILEASNGLYGLUARGASP
6   GLUILEARGVALARGASNILESERLYSGLU
7   GLULEULYSLYSLEULEUGLUARGILEARG
8   GLULYSILEGLUARGGLUGLYSERSERGLU
9   VALGLUVALASNVALHISSERGLYGLYGLN
10   THRTRPTHRPHEASNGLULYS

Samples:

sample_1: foldit3, [U-13C; U-15N], 0.3 ± 0.05 mM

sample_conditions_1: ionic strength: 0.2 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

AutoStructure, Huang, Tejero, Powers and Montelione - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

SPARKY, Goddard - peak picking

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

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AvanceIII 600 MHz

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