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Biological Magnetic Resonance Data Bank


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BMRB Entry 18429

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18429
MolProbity Validation Chart

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Title: Solution NMR Structure of De Novo Designed Four Helix Bundle Protein, Northeast Structural Genomics Consortium (NESG) Target OR188

Deposition date: 2012-04-28 Original release date: 2012-08-30

Authors: Sathyamoorthy, Bharathwaj; Pulavarti, Surya VSRK; Murphy, Grant; Mills, Jeffrey; Eletski, Alexander; Der, Bryan; Machius, Mischa; Kuhlman, Brian; Montelione, Gaetano; Szyperski, Thomas

Citation: Murphy, Grant; Sathyamoorthy, Bharathwaj; Der, Bryan; Machius, Mischa; Pulavarti, Surya VSRK; Montelione, Gaetano; Szyperski, Thomas; Kuhlman, Brian. "Solution NMR Structure of a Denovo Design Four Helix Bundle Protein, Northeast Structural Genomics Consortium Target OR188"  To be published ., .-..

Assembly members:
OR188, polymer, 101 residues, 11927.662 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):
OR188: MQEERKKLLEKLEKILDEVT DGAPDEARERIEKLAKDVKD ELEEGDAKNMIEKFRDEMEQ MYKDAPNAVMEQLLEEIEKL LKKAGSLVPRGSYLEHHHHH H

Data sets:
Data typeCount
13C chemical shifts435
15N chemical shifts95
1H chemical shifts717

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1OR1881

Entities:

Entity 1, OR188 101 residues - 11927.662 Da.

1   METGLNGLUGLUARGLYSLYSLEULEUGLU
2   LYSLEUGLULYSILELEUASPGLUVALTHR
3   ASPGLYALAPROASPGLUALAARGGLUARG
4   ILEGLULYSLEUALALYSASPVALLYSASP
5   GLULEUGLUGLUGLYASPALALYSASNMET
6   ILEGLULYSPHEARGASPGLUMETGLUGLN
7   METTYRLYSASPALAPROASNALAVALMET
8   GLUGLNLEULEUGLUGLUILEGLULYSLEU
9   LEULYSLYSALAGLYSERLEUVALPROARG
10   GLYSERTYRLEUGLUHISHISHISHISHIS
11   HIS

Samples:

NC: OR188.001, [U-100% 13C; U-100% 15N], 23.8 mg/mL; phosphate 100 mM; NaCl 100 mM; H2O 90%; D2O 10%

NC10: OR188.001, [U-10% 13C; U-100% 15N], 1.3 mg/mL; phosphate 100 mM; NaCl 100 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_1
3D HN(CA)CONCisotropicsample_conditions_1
3D HNCONCisotropicsample_conditions_1
(4,3)D GFT CABCA(CO)NHNCisotropicsample_conditions_1
(4,3)D GFT HNCACABNCisotropicsample_conditions_1
(4,3)D GFT HABCAB(CO)NHNCisotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYNCisotropicsample_conditions_1
2D 1H-13C HSQC aliphatic CTNCisotropicsample_conditions_1
2D 1H-13C HSQC aromatic CTNCisotropicsample_conditions_1
(4,3)D GFT HCCH-COSY aliphatic SP1/SP2/CPNCisotropicsample_conditions_1
3D HCCH TOCSYNCisotropicsample_conditions_1
3D C(CO)NHNCisotropicsample_conditions_1
3D H(CCO)NHNCisotropicsample_conditions_1
(4,3)D GFT HCCH-COSY aromatic SP1/SP2/CPNCisotropicsample_conditions_1
2D 1H-13C HSQC aliphatic 28ms CTNC10isotropicsample_conditions_1
2D 1H-13C HSQC aliphatic 42ms CTNC10isotropicsample_conditions_1
2D 1H-13C HSQC aliphatic 56ms CTNC10isotropicsample_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

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

PROSA, Guntert - processing

XEASY, Bartels et al. - data analysis, processing

VNMRJ v2.2D, Varian - collection

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

PSVS, Bhattacharya, Montelione - structure validation

CARA v1,8, Keller and Wuthrich - chemical shift assignment, chemical shift calculation, data analysis, peak picking, refinement

CSI v2.0, David Wishart, Brian Sykes - data analysis

Molmol v2K.2, Koradi, Billeter and Wuthrich - structure solution, visualization

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz

Related Database Links:

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Download simulated HSQC data in one of the following formats:
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