BMRB Entry 17612

Name: Solution NMR Structure of a Protein With a Redesigned Hydrophobic Core, Northeast Structural Genomics Consortium Target OR38
Published: 2011-06-01

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PDB ID: 2lch
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17612
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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:

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:

Assembly members:
OR38, polymer, 113 residues, 13266.547 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: pet21b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
OR38: MGSHQEYIKKVTDELKELIQ NVNDDIKEVEKNPEDMEYWN KIYRLVHTMKEITETMGFSS VAKVLHTIMNLVDKMLNSEI KITSDLIDKVKKKLDMVTRE LDKKVSGSYLVPR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	489
15N chemical shifts	112
1H chemical shifts	835

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	OR38	1

Entities:

Entity 1, OR38 113 residues - 13266.547 Da.

1

MET

GLY

SER

HIS

GLN

GLU

TYR

ILE

LYS

2

VAL

THR

ASP

GLU

LEU

LYS

GLU

LEU

ILE

GLN

3

ASN

VAL

ASN

ASP

ILE

LYS

GLU

VAL

GLU

4

LYS

ASN

PRO

GLU

ASP

MET

GLU

TYR

TRP

ASN

5

LYS

ILE

TYR

ARG

LEU

VAL

HIS

THR

MET

LYS

6

GLU

ILE

THR

GLU

THR

MET

GLY

PHE

SER

7

VAL

ALA

LYS

VAL

LEU

HIS

THR

ILE

MET

ASN

8

LEU

VAL

ASP

LYS

MET

LEU

ASN

SER

GLU

ILE

9

LYS

ILE

THR

SER

ASP

LEU

ILE

ASP

LYS

VAL

10

LYS

LEU

ASP

MET

VAL

THR

ARG

GLU

11

LEU

ASP

LYS

VAL

SER

GLY

SER

TYR

LEU

12

VAL

PRO

ARG

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	NC	isotropic	sample_conditions_1
2D 1H-13C HSQC	NC	isotropic	sample_conditions_1
3D HNCO	NC	isotropic	sample_conditions_1
3D CBCA(CO)NH	NC	isotropic	sample_conditions_1
3D HNCACB	NC	isotropic	sample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY	NC	isotropic	sample_conditions_1
3D HBHA(CO)NH	NC	isotropic	sample_conditions_1
3D HCCH-TOCSY	NC	isotropic	sample_conditions_1
3D HCCH-COSY	NC	isotropic	sample_conditions_1
2D 1H-15N HSQC	NC5	isotropic	sample_conditions_1
3D HN(CA)CO	NC	isotropic	sample_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