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 25062

Title: Solution NMR Structure of De novo designed protein, Northeast Structural Genomics Consortium (NESG) Target OR462

Authors: Xu, Xianzhong; Nivon, Lucas; Federizon, Jasmin; Maglaqui, Melissa; Janjua, Haleema; Mao, Lei; Xiao, Rong; Kornhaber, Gregory; Baker, David; Montelione, Gaetano; Szyperski, Thomas

Citation: Xu, Xianzhong; Nivon, Lucas; Federizon, Jasmin; Maglaqui, Melissa; Janjua, Haleema; Mao, Lei; Xiao, Rong; Kornhaber, Gregory; Baker, David; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of De novo designed protein, Northeast Structural Genomics Consortium (NESG) Target OR462"  To be published ., .-..

Assembly members:
OR462, polymer, 136 residues, 15713.062 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):
OR462: MGVVILVLTGDERIAEELRK EVQKHDPNVKTVPTKDKEKV KEEIEKARKQGRPIVVFVRG GDDERAKDIAEYAQKEGLRV IVIIVSQDEEALRKGYEDKK KKGYDVYTSRNEDEAKKKLK EALEKSGSLEHHHHHH

Data typeCount
13C chemical shifts602
15N chemical shifts136
1H chemical shifts969

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1OR4621

Entities:

Entity 1, OR462 136 residues - 15713.062 Da.

Residues 1-128 correspond to the De novo designed active lysine protein. Residues 129-136 represent a purification his-tag.

1   METGLYVALVALILELEUVALLEUTHRGLY
2   ASPGLUARGILEALAGLUGLULEUARGLYS
3   GLUVALGLNLYSHISASPPROASNVALLYS
4   THRVALPROTHRLYSASPLYSGLULYSVAL
5   LYSGLUGLUILEGLULYSALAARGLYSGLN
6   GLYARGPROILEVALVALPHEVALARGGLY
7   GLYASPASPGLUARGALALYSASPILEALA
8   GLUTYRALAGLNLYSGLUGLYLEUARGVAL
9   ILEVALILEILEVALSERGLNASPGLUGLU
10   ALALEUARGLYSGLYTYRGLUASPLYSLYS
11   LYSLYSGLYTYRASPVALTYRTHRSERARG
12   ASNGLUASPGLUALALYSLYSLYSLEULYS
13   GLUALALEUGLULYSSERGLYSERLEUGLU
14   HISHISHISHISHISHIS

Samples:

NC5: OR462, [U-13C; U-15N], 1.2 mM

NC: OR462, [U-13C; U-15N], 1.2 mM

sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_1
2D 1H-13C HSQC aromaticNCisotropicsample_conditions_1
3D HNCONCisotropicsample_conditions_1
3D CBCA(CO)NHNCisotropicsample_conditions_1
3D HNCACBNCisotropicsample_conditions_1
3D HBHA(CO)NHNCisotropicsample_conditions_1
3D simultaneous Cali,Caro, and N NOESYNCisotropicsample_conditions_1
CCH-TOCSYNCisotropicsample_conditions_1
3D HN(CA)CONCisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticNCisotropicsample_conditions_1
2D ct-1H-13C HSQC aliphaticNCisotropicsample_conditions_1
2D ct-1H-13C HSQC aromaticNCisotropicsample_conditions_1
GFT(4,3d) HCCHCOSY aliNCisotropicsample_conditions_1
gft(4,3d) HCCHCOSY caroNCisotropicsample_conditions_1
2D ct-1H-13C HSQC aliphatic 28msNC5isotropicsample_conditions_1
2D ct-1H-13C hsqc aliphatic 28msNC5isotropicsample_conditions_1
2D ct-1H-13C hscq aliphatic 42msNC5isotropicsample_conditions_1
2D cr-1H-13C hsqc aliphatic 56msNC5isotropicsample_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 v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

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

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

TALOSN, Shen, Cornilescu, Delaglio and Bax - geometry optimization

AS-DP v1.0, (AS-DP) Huang,Tejero,Powers, and Montelione - data analysis, structure solution

Cara v1.8.4, Keller and Wuthrich - chemical shift assignment, peak picking

PSVS, Bhattacharya, Montelione - structure validation

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz

Related Database Links:

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