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 25612

Title: Solution NMR Structure of DE NOVO DESIGNED Ferredoxin Fold PROTEIN sfr3, Northeast Structural Genomics Consortium (NESG) Target OR358

Deposition date: 2015-05-14 Original release date: 2015-09-14

Authors: Liu, Gaohua; Lin, Yu-Ru; Koga, Nobuyasu; Koga, Rie; Xiao, Rong; Janjua, Haleema; Hamilton, Keith; 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; Hamilton, Keith; Pederson, Kari; Acton, Thomas; Kornhaber, Gregory; Everett, John; Baker, David; Montelione, Gaetano. "Solution NMR Structure of DE NOVO DESIGNED Ferredoxin Fold PROTEIN sfr3, Northeast Structural Genomics Consortium (NESG) Target OR358"  To be published ., .-..

Assembly members:
OR358, polymer, 77 residues, 8898.169 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):
OR358: MVDLKIDVSDDEEAEKIIRE IREQWPKATVTRTNGDIKLD AQTEKEAEKMEKAVKKVKPN ATIRKTGGSLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts306
15N chemical shifts70
1H chemical shifts508
residual dipolar couplings47

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1OR3581

Entities:

Entity 1, OR358 77 residues - 8898.169 Da.

1   METVALASPLEULYSILEASPVALSERASP
2   ASPGLUGLUALAGLULYSILEILEARGGLU
3   ILEARGGLUGLNTRPPROLYSALATHRVAL
4   THRARGTHRASNGLYASPILELYSLEUASP
5   ALAGLNTHRGLULYSGLUALAGLULYSMET
6   GLULYSALAVALLYSLYSVALLYSPROASN
7   ALATHRILEARGLYSTHRGLYGLYSERLEU
8   GLUHISHISHISHISHISHIS

Samples:

sample_NC5: OR358, [U-13C; U-15N], 0.787 mM; H20 90%; D20 10%

sample_RDC: OR358, [U-13C; U-15N], 0.787 mM; H20 90%; D20 10%

sample_NC: OR358, [U-13C; U-15N], 0.787 mM; H20 90%; D20 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
3D CCH-TOCSYsample_NCisotropicsample_conditions_1
2D 1H-15N HSQCsample_RDCisotropicsample_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

PALES, PALES (Zweckstetter, 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