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 17304

Title: Solution NMR Structure of de novo designed rossmann 2x3 fold protein, Northeast Structural Genomics Consortium Target OR28   PubMed: 34168113

Deposition date: 2010-11-17 Original release date: 2010-12-16

Authors: Liu, Gaohua; Koga, Nobuyasu; Koga, Rie; Xiao, Rong; Mao, Lei; Mao, binchen; Patel, Daya; ciccosanti, colleen; Hamilton, Keith; Acton, Thomas; Baker, David; Montelione, Gaetano

Citation: Koga, N.; Koga, R.; Liu, G.; Castellanos, J.; Montelione, G.; Baker, D.. "Role of backbone strain in de novo design of complex alpha/beta protein structures"  Nat. Commun. 12, 3921-3921 (2021).

Assembly members:
OR28, polymer, 134 residues, 15857.373 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   Vector: pET29b+

Entity Sequences (FASTA):
OR28: MNIVIVVFSTDEETLRKFKD IIKKNGFKVRTVRSPQELKD SIEELVKKYNATIVVVVVDD KEWAEKAIRFVKSLGAQVLI IIYDQDQNRLEEFSREVRRR GFEVRTVTSPDDFKKSLERL IREVGSLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts481
15N chemical shifts132
1H chemical shifts975

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1OR281

Entities:

Entity 1, OR28 134 residues - 15857.373 Da.

1   METASNILEVALILEVALVALPHESERTHR
2   ASPGLUGLUTHRLEUARGLYSPHELYSASP
3   ILEILELYSLYSASNGLYPHELYSVALARG
4   THRVALARGSERPROGLNGLULEULYSASP
5   SERILEGLUGLULEUVALLYSLYSTYRASN
6   ALATHRILEVALVALVALVALVALASPASP
7   LYSGLUTRPALAGLULYSALAILEARGPHE
8   VALLYSSERLEUGLYALAGLNVALLEUILE
9   ILEILETYRASPGLNASPGLNASNARGLEU
10   GLUGLUPHESERARGGLUVALARGARGARG
11   GLYPHEGLUVALARGTHRVALTHRSERPRO
12   ASPASPPHELYSLYSSERLEUGLUARGLEU
13   ILEARGGLUVALGLYSERLEUGLUHISHIS
14   HISHISHISHIS

Samples:

sample_NC: OR28, [U-100% 13C; U-100% 15N], 0.62 mM; H2O 95%; D2O 5%

sample_NC5: OR28, [U-5% 13C; U-100% 15N], 0.47 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_NCisotropicsample_conditions_1
2D 1H-13C HSQCsample_NC5isotropicsample_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

Software:

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

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

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

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

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

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

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

UBNMR v1.3, Yang Shen - data analysis

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

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

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