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 25662

Title: Solution NMR Structure of DE NOVO DESIGNED PROTEIN, Rossmann2x2 Fold, Northeast Structural Genomics Consortium (NESG) Target OR446

Deposition date: 2015-06-15 Original release date: 2015-09-14

Authors: Liu, Gaohua; Lin, Yu-Ru; Koga, Nobuyasu; Koga, Rie; Xiao, Rong; Janjua, Haleema; Pederson, Kari; Acton, Thomas; Kornhaber, Gregory; Everett, John; Baker, David; Montelione, Gaetano

Citation: Liu, Gaohua; Lin, Yu-Ru; Koga, Nobuyasu; Koga, Rie; Xiao, Rong; Janjua, Haleema; Pederson, Kari; Acton, Thomas; Kornhaber, Gregory; Everett, John; Baker, David; Montelione, Gaetano. "Solution NMR Structure of DE NOVO DESIGNED PROTEIN, Rossmann2x2 Fold, Northeast Structural Genomics Consortium (NESG) Target OR446"  To be published ., .-..

Assembly members:
OR446, polymer, 99 residues, 11377.278 Da.

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):
OR446: MGRLVVVVTSEQLKEEVRKK FPQVEVRLVTTEEDAKQVIK EIQKKGVQKVVLVGVSEKLL QKIKQEANVQVYRVTSNDEL EQVVKDVKGSGLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts422
15N chemical shifts99
1H chemical shifts721
residual dipolar couplings136

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1OR4461

Entities:

Entity 1, OR446 99 residues - 11377.278 Da.

1   METGLYARGLEUVALVALVALVALTHRSER
2   GLUGLNLEULYSGLUGLUVALARGLYSLYS
3   PHEPROGLNVALGLUVALARGLEUVALTHR
4   THRGLUGLUASPALALYSGLNVALILELYS
5   GLUILEGLNLYSLYSGLYVALGLNLYSVAL
6   VALLEUVALGLYVALSERGLULYSLEULEU
7   GLNLYSILELYSGLNGLUALAASNVALGLN
8   VALTYRARGVALTHRSERASNASPGLULEU
9   GLUGLNVALVALLYSASPVALLYSGLYSER
10   GLYLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: OR446.003 1.34 mM; D2O 10%; H2O 90%

sample_2: OR446.003 1.34 mM; D2O 10%; H2O 90%

sample_3: OR446.003 1.34 mM; D2O 10%; H2O 90%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D 1H-13C arom NOESYsample_3isotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYsample_3isotropicsample_conditions_1
3D CCH-TOCSYsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution

AutoStructure v2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

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

XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

SPARKY, Goddard - data analysis

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

REDCAT, Valafar, Prestegard - geometry optimization

PSVS, Bhattacharya, Montelione - structure validation

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 600 MHz

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