BMRB Entry 17390

Title:
Solution NMR Structure of de novo designed protein, P-loop NTPase fold, Northeast Structural Genomics Consortium Target OR32
Deposition date:
2010-12-31
Original release date:
2011-01-24
Authors:
Liu, Gaohua; Koga, Nobuyasu; Koga, Rie; Xiao, Rong; Hamilton, Keith; Janjua, Haleema; Tong, Saichu; Acton, Thomas; Everett, John; Baker, David; Montelione, Gaetano
Citation:

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).
PubMed: 34168113

Assembly members:

Assembly members:
OR32, polymer, 162 residues, 19701.238 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET29b+

Data sets:
Data typeCount
13C chemical shifts584
15N chemical shifts173
1H chemical shifts1181

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1OR321

Entities:

Entity 1, OR32 162 residues - 19701.238 Da.

1   METSERGLNILEPHEVALVALPHESERSER
2   ASPPROGLUILELEULYSGLUILEVALARG
3   GLUILELYSARGGLNGLYVALARGVALVAL
4   LEULEUTYRSERASPGLNASPGLULYSARG
5   ARGARGGLUARGLEUGLUGLUPHEGLULYS
6   GLNGLYVALASPVALARGTHRVALGLUASP
7   LYSGLUASPPHEARGGLUASNILEARGGLU
8   ILETRPGLUARGTYRPROGLNLEUASPVAL
9   VALVALILEVALTHRTHRASPASPLYSGLU
10   TRPILELYSASPPHEILEGLUGLUALALYS
11   GLUARGGLYVALGLUVALPHEVALVALTYR
12   ASNASNLYSASPASPASPARGARGLYSGLU
13   ALAGLNGLNGLUPHEARGSERASPGLYVAL
14   ASPVALARGTHRVALSERASPLYSGLUGLU
15   LEUILEGLUGLNVALARGARGPHEVALARG
16   LYSVALGLYSERLEUGLUHISHISHISHIS
17   HISHIS

Samples:

sample_NC: OR32, [U-100% 13C; U-100% 15N], 1.06 mM; H2O 90%; D2O 10%

sample_NC5: OR32, [U-5% 13C; U-100% 15N], 0.85 mM; H2O 90%; D2O 10%

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_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
2D 1H-15N HSQCsample_NC5isotropicsample_conditions_1
3D HBHA(CO)NHsample_NCisotropicsample_conditions_1
3D C(CO)NHsample_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

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY, Goddard - data analysis

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

PALES, PALES (Zweckstetter, Bax) - geometry optimization

REDCAT, Valafar, Prestegard - 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 peaks
SPARKY: Backbone or all simulated peaks