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 18145

Title: Solution NMR Structure of DE NOVO DESIGNED PROTEIN, IF3-like fold, Northeast Structural Genomics Consortium Target OR135 (CASD target)   PubMed: 23135467

Authors: Liu, Gaohua; Koga, Nobuyasu; Koga, Rie; Xiao, Rong; Lee, Hsiau-Wei; Janjua, Haleema; Kohan, Eitan; Acton, Thomas; Everett, John; Baker, David; Montelione, Gaetano

Citation: Koga, Nobuyasu; Tatsumi-Koga, Rie; Liu, Gaohua; Xiao, Rong; Acton, Thomas; Montelione, Gaetano; Baker, David. "Principles for designing ideal protein structures"  Nature 491, 222-227 (2012).

Assembly members:
OR135, polymer, 83 residues, 9797.112 Da.

Natural source:   Common Name: not available   Taxonomy ID: 32644   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):
OR135: MGLTRTITSQNKEELLEIAL KFISQGLDLEVEFDSTDDKE IEEFERDMEDLAKKTGVQIQ KQWQGNKLRIRLKGSLEHHH HHH

Data sets:
Data typeCount
13C chemical shifts351
15N chemical shifts85
1H chemical shifts580
residual dipolar couplings116

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1OR1351

Entities:

Entity 1, OR135 83 residues - 9797.112 Da.

1   METGLYLEUTHRARGTHRILETHRSERGLN
2   ASNLYSGLUGLULEULEUGLUILEALALEU
3   LYSPHEILESERGLNGLYLEUASPLEUGLU
4   VALGLUPHEASPSERTHRASPASPLYSGLU
5   ILEGLUGLUPHEGLUARGASPMETGLUASP
6   LEUALALYSLYSTHRGLYVALGLNILEGLN
7   LYSGLNTRPGLNGLYASNLYSLEUARGILE
8   ARGLEULYSGLYSERLEUGLUHISHISHIS
9   HISHISHIS

Samples:

sample_NC: OR135, [U-100% 13C; U-100% 15N], 1.04 mM; H20 95%; D20 5%

sample_NC5: OR135, [U-5% 13C; U-100% 15N], 1.14 mM; H2O 95%; D2O 5%

sample_NC5_RDC: OR135, [U-5% 13C; U-100% 15N], 1.14 mM; OR135 95%; OR135 5%

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_NCisotropicsample_conditions_1
2D 1H-13C HSQCsample_NCisotropicsample_conditions_1
3D HNCOsample_NCisotropicsample_conditions_1
3D CBCA(CO)NHsample_NCisotropicsample_conditions_1
3D HNCACBsample_NCisotropicsample_conditions_1
3D 1H-13C arom NOESYsample_NCisotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYsample_NCisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_NC5isotropicsample_conditions_1
2D 1H-15N HSQCsample_NC5isotropicsample_conditions_1
3D HCCH-TOCSYsample_NCisotropicsample_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

AutoStruct 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

NMR spectrometers:

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

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