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Biological Magnetic Resonance Data Bank


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BMRB Entry 17612

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17612
MolProbity Validation Chart

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Title: Solution NMR Structure of a Protein With a Redesigned Hydrophobic Core, Northeast Structural Genomics Consortium Target OR38

Deposition date: 2011-04-29 Original release date: 2011-06-01

Authors: Mills, Jeffrey; Murphy, Grant; Miley, Mike; Machius, Mischa; Kuhlman, Brian; Szyperski, Thomas

Citation: Mills, Jeffrey; Murphy, Grant; Miley, Mike; Machius, Mischa; Kuhlman, Brian; Szyperski, Thomas. "Solution NMR Structure of a Protein With a Redesigned Hydrophobic Core, Northeast Structural Genomics Consortium Target OR38"  To be published ., .-..

Assembly members:
OR38, polymer, 113 residues, 13266.547 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):
OR38: MGSHQEYIKKVTDELKELIQ NVNDDIKEVEKNPEDMEYWN KIYRLVHTMKEITETMGFSS VAKVLHTIMNLVDKMLNSEI KITSDLIDKVKKKLDMVTRE LDKKVSGSYLVPR

Data sets:
Data typeCount
13C chemical shifts489
15N chemical shifts112
1H chemical shifts835

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1OR381

Entities:

Entity 1, OR38 113 residues - 13266.547 Da.

1   METGLYSERHISGLNGLUTYRILELYSLYS
2   VALTHRASPGLULEULYSGLULEUILEGLN
3   ASNVALASNASPASPILELYSGLUVALGLU
4   LYSASNPROGLUASPMETGLUTYRTRPASN
5   LYSILETYRARGLEUVALHISTHRMETLYS
6   GLUILETHRGLUTHRMETGLYPHESERSER
7   VALALALYSVALLEUHISTHRILEMETASN
8   LEUVALASPLYSMETLEUASNSERGLUILE
9   LYSILETHRSERASPLEUILEASPLYSVAL
10   LYSLYSLYSLEUASPMETVALTHRARGGLU
11   LEUASPLYSLYSVALSERGLYSERTYRLEU
12   VALPROARG

Samples:

NC: OR38, [U-100% 13C; U-100% 15N], 1.0 mM; sodium phosphate 100 mM; sodium chloride 50 mM; H2O 95%; D2O 5%

NC5: OR38, [U-10% 13C; U-100% 15N], 1.0 mM; sodium phosphate 100 mM; sodium chloride 50 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_1
2D 1H-13C HSQCNCisotropicsample_conditions_1
3D HNCONCisotropicsample_conditions_1
3D CBCA(CO)NHNCisotropicsample_conditions_1
3D HNCACBNCisotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYNCisotropicsample_conditions_1
3D HBHA(CO)NHNCisotropicsample_conditions_1
3D HCCH-TOCSYNCisotropicsample_conditions_1
3D HCCH-COSYNCisotropicsample_conditions_1
2D 1H-15N HSQCNC5isotropicsample_conditions_1
3D HN(CA)CONCisotropicsample_conditions_1

Software:

CARA v1.8, Keller et al. - chemical shift assignment, data analysis, peak picking

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

VNMRJ, Varian - collection

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

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

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Varian INOVA 750 MHz

Related Database Links:

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Download simulated HSQC data in one of the following formats:
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