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 25067

Title: Solution NMR Structure of De novo designed protein, Northeast Structural Genomics Consortium (NESG) Target OR459

Authors: Pulavarti, Surya VSRK; Kipnis, Yakov; Sukumaran, Dinesh; Maglaqui, Melissa; Janjua, Haleema; Mao, Lei; Xiao, Rong; Kornhaber, Greg; Baker, David; Montelione, Gaetano; Szyperski, Thomas

Citation: Pulavarti, Surya VSRK; Kipnis, Yakov; Sukumaran, Dinesh; Maglaqui, Melissa; Janjua, Haleema; Mao, Lei; Xiao, Rong; Kornhaber, Greg; Baker, David; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of De novo designed protein, Northeast Structural Genomics Consortium (NESG) Target OR459"  To be published ., .-..

Assembly members:
OR459, polymer, 117 residues, 13406.451 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):
OR459: MAGKELRVEIKIDCGNDDKE TTYDLYFSKAEEAKELLKKV AEKAADKIKKQGCKRVKIRF EKKGLDDDARKKAKKWALEV ANKIANELGAKQSTTTTDGD TFEVEVILELEHHHHHH

Data sets:
Data typeCount
1H chemical shifts782
13C chemical shifts486
15N chemical shifts104

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1OR4591

Entities:

Entity 1, OR459 117 residues - 13406.451 Da.

1   METALAGLYLYSGLULEUARGVALGLUILE
2   LYSILEASPCYSGLYASNASPASPLYSGLU
3   THRTHRTYRASPLEUTYRPHESERLYSALA
4   GLUGLUALALYSGLULEULEULYSLYSVAL
5   ALAGLULYSALAALAASPLYSILELYSLYS
6   GLNGLYCYSLYSARGVALLYSILEARGPHE
7   GLULYSLYSGLYLEUASPASPASPALAARG
8   LYSLYSALALYSLYSTRPALALEUGLUVAL
9   ALAASNLYSILEALAASNGLULEUGLYALA
10   LYSGLNSERTHRTHRTHRTHRASPGLYASP
11   THRPHEGLUVALGLUVALILELEUGLULEU
12   GLUHISHISHISHISHISHIS

Samples:

sample_1: H2O 90 ± 0.005 %; D2O 10%; OR459.005, [U-13C,15N], 1.17 mM

sample_2: H2O 90%; D2O 10%; OR459.005, [5% 13C; U-15N], 1.17 mM

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
GFT-4,3d-hcch-COSYsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_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

CARA, Rochus Keller - Analysis

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

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

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

PSVS, Bhattacharya, Montelione - structure validation

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz

Related Database Links:

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