BMRB Entry 18145

Name: Solution NMR Structure of DE NOVO DESIGNED PROTEIN, IF3-like fold, Northeast Structural Genomics Consortium Target OR135 (CASD target)
Published: 2012-01-31

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PDB ID: 2ln3
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18145
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR Structure of DE NOVO DESIGNED PROTEIN, IF3-like fold, Northeast Structural Genomics Consortium Target OR135 (CASD target)

Deposition date:

2011-12-15

Original release date:

2012-01-31

Authors:

Liu, Gaohua; Koga, Nobuyasu; Koga, Rie; Xiao, Rong; Lee, Hsiau-Wei; Janjua, Haleema; Kohan, Eitan; Acton, Thomas; Everett, John; Baker, David; Montelione, Gaetano

Citation:

Citation: Koga, Nobuyasu; Tatsumi-Koga, Rie; Liu, Gaohua; Xiao, Rong; Acton, Thomas; Montelione, Gaetano; Baker, David. "Principles for designing ideal protein structures" Nature 491, 222-227 (2012).
PubMed: 23135467

Assembly members:

Assembly members:
OR135, polymer, 83 residues, 9797.112 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: 32644 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: pET29b+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
OR135: MGLTRTITSQNKEELLEIAL KFISQGLDLEVEFDSTDDKE IEEFERDMEDLAKKTGVQIQ KQWQGNKLRIRLKGSLEHHH HHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
RDCs
- RDC_list_1
- RDC_list_2

Data type	Count
13C chemical shifts	351
15N chemical shifts	85
1H chemical shifts	580
residual dipolar couplings	116

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	OR135	1

Entities:

Entity 1, OR135 83 residues - 9797.112 Da.

1

MET

GLY

LEU

THR

ARG

THR

ILE

THR

SER

GLN

2

ASN

LYS

GLU

LEU

GLU

ILE

ALA

LEU

3

LYS

PHE

ILE

SER

GLN

GLY

LEU

ASP

LEU

GLU

4

VAL

GLU

PHE

ASP

SER

THR

ASP

LYS

GLU

5

ILE

GLU

PHE

GLU

ARG

ASP

MET

GLU

ASP

6

LEU

ALA

LYS

THR

GLY

VAL

GLN

ILE

GLN

7

LYS

GLN

TRP

GLN

GLY

ASN

LYS

LEU

ARG

ILE

8

ARG

LEU

LYS

GLY

SER

LEU

GLU

HIS

9

HIS

Samples:

sample_NC: OR135, [U-100% 13C; U-100% 15N], 1.04 mM; H20 95%; D20 5%

sample_NC5: OR135, [U-5% 13C; U-100% 15N], 1.14 mM; H2O 95%; D2O 5%

sample_NC5_RDC: OR135, [U-5% 13C; U-100% 15N], 1.14 mM; OR135 95%; OR135 5%

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

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_NC	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_NC	isotropic	sample_conditions_1
3D HNCO	sample_NC	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_NC	isotropic	sample_conditions_1
3D HNCACB	sample_NC	isotropic	sample_conditions_1
3D 1H-13C arom NOESY	sample_NC	isotropic	sample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY	sample_NC	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_NC5	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_NC5	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_NC	isotropic	sample_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

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

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

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

SPARKY, Goddard - data analysis

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

REDCAT, Valafar, Prestegard - geometry optimization

NMR spectrometers:

Bruker Avance 800 MHz
Varian INOVA 600 MHz
Varian INOVA 600 MHz