BMRB Entry 25611

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25611
MolProbity Validation Chart

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Title:
Solution NMR Structure of DE NOVO DESIGNED PROTEIN (FDA_60), Northeast Structural Genomics Consortium (NESG) Target OR303
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; 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; Hamilton, Keith; Acton, Thomas; Kornhaber, Gregory; Everett, John; Baker, David; Montelione, Gaetano. "Solution NMR Structure of DE NOVO DESIGNED PROTEIN (FDA_60), Northeast Structural Genomics Consortium (NESG) Target OR303"  To be published ., .-..

Assembly members:

Assembly members:
OR303, polymer, 84 residues, 10337.523 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
OR303: MGQWQIKIYSENEREFRELI ERLEEERPSVQYTETTRNGR RQLTIRSNDKNEVDRILEEV RRKVPNARVRETETGSLEHH HHHH

Data sets:
Data typeCount
13C chemical shifts366
15N chemical shifts96
1H chemical shifts599

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1OR3031

Entities:

Entity 1, OR303 84 residues - 10337.523 Da.

1   METGLYGLNTRPGLNILELYSILETYRSER
2   GLUASNGLUARGGLUPHEARGGLULEUILE
3   GLUARGLEUGLUGLUGLUARGPROSERVAL
4   GLNTYRTHRGLUTHRTHRARGASNGLYARG
5   ARGGLNLEUTHRILEARGSERASNASPLYS
6   ASNGLUVALASPARGILELEUGLUGLUVAL
7   ARGARGLYSVALPROASNALAARGVALARG
8   GLUTHRGLUTHRGLYSERLEUGLUHISHIS
9   HISHISHISHIS

Samples:

sample: OR303.005, [U-100% 13C; U-100% 15N], 0.87 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 4.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsampleisotropicsample_conditions_1
2D 1H-13C HSQCsampleisotropicsample_conditions_1
3D HNCOsampleisotropicsample_conditions_1
3D CBCA(CO)NHsampleisotropicsample_conditions_1
3D HNCACBsampleisotropicsample_conditions_1
3D 1H-13C arom NOESYsampleisotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYsampleisotropicsample_conditions_1

Software:

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

PSVS, Bhattacharya, Montelione - structure validation

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