BMRB Entry 25018

Title:
Solution NMR Structure of DE NOVO DESIGNED PROTEIN LFR1 WITH FERREDOXIN FOLD, Northeast Structural Genomics Consortium (NESG) Target OR414
Deposition date:
2014-06-12
Original release date:
2014-08-25
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:

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 LFR1 1WITH FERREDOXIN FOLD, Northeast Structural Genomics Consortium (NESG) Target OR414"  To be published ., .-..

Assembly members:

Assembly members:
OR414, polymer, 112 residues, 13116.892 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: pET21_NESG

Data typeCount
13C chemical shifts475
15N chemical shifts107
1H chemical shifts784
residual dipolar couplings82

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1OR4141

Entities:

Entity 1, OR414 112 residues - 13116.892 Da.

1   METLEUTHRVALGLUVALGLUVALLYSILE
2   THRALAASPASPGLUASNLYSALAGLUGLU
3   ILEVALLYSARGVALILEASPGLUVALGLU
4   ARGGLUVALGLNLYSGLNTYRPROASNALA
5   THRILETHRARGTHRLEUTHRARGASPASP
6   GLYTHRVALGLULEUARGILELYSVALLYS
7   ALAASPTHRGLUGLULYSALALYSSERILE
8   ILELYSLEUILEGLUGLUARGILEGLUGLU
9   GLULEUARGLYSARGASPPROASNALATHR
10   ILETHRARGTHRVALARGTHRGLUVALGLY
11   SERSERTRPSERLEUGLUHISHISHISHIS
12   HISHIS

Samples:

sample_NC: OR414, [U-99% 13C; U-98% 15N], 0.885 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_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
3D CCH-TOCSYsample_NCisotropicsample_conditions_1
2D 1H-13C HSQCsample_NCisotropicsample_conditions_1
2D 1H-15N HSQCsample_NCisotropicsample_conditions_1

Software:

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

AutoStructure 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

SPARKY, Goddard - data analysis

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

REDCAT, Valafar, Prestegard - geometry optimization

PSVS, Bhattacharya, Montelione - structure validation

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

NMR spectrometers:

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

Related Database Links:

PDB

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