BMRB Entry 25664

Name: Solution NMR Structure of DE NOVO DESIGNED PROTEIN Top7NNSTYCC, Northeast Structural Genomics Consortium (NESG) Target OR34
Published: 2016-02-29

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PDB ID: 2n41
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25664
MolProbity Validation Chart

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR Structure of DE NOVO DESIGNED PROTEIN Top7NNSTYCC, Northeast Structural Genomics Consortium (NESG) Target OR34

Deposition date:

2016-02-29

Original release date:

2016-02-29

Authors:

Liu, Gaohua; Chan, Kui; Basanta, Benjamin; Xiao, Rong; Janjua, Haleema; Kogan, Sam; Maglaqui, Melissa; Ciccosanti, Colleen; Acton, Thomas; Kornhaber, Gregory; Everett, John; Baker, David; Montelione, Gaetano

Citation:

Citation: Liu, Gaohua; Chan, Kui; Basanta, Benjamin; Xiao, Rong; Janjua, Haleema; Kogan, Sam; Maglaqui, Melissa; Ciccosanti, Colleen; Acton, Thomas; Kornhaber, Gregory; Everett, John; Baker, David; Montelione, Gaetano. "Solution NMR Structure of DE NOVO DESIGNED PROTEIN Top7NNSTYCC, Northeast Structural Genomics Consortium (NESG) Target OR34" To be published ., .-..

Assembly members:

Assembly members:
OR34, polymer, 106 residues, 12146.624 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: pET29b+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
OR34: MHHHHHHRSGDIQVQNNNTC NGKTFDYTYTVTTESELQKV LNELKDYIKKQGCKRSRTSI TARTKKEAEKFAAILIKVYA ELGYNDINVTWDGDTVTVEG QLEGVD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
13C chemical shifts	301
15N chemical shifts	85
1H chemical shifts	625

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	OR34	1

Entities:

Entity 1, OR34 106 residues - 12146.624 Da.

1

MET

HIS

ARG

SER

GLY

2

ASP

ILE

GLN

VAL

GLN

ASN

THR

CYS

3

ASN

GLY

LYS

THR

PHE

ASP

TYR

THR

TYR

THR

4

VAL

THR

GLU

SER

GLU

LEU

GLN

LYS

VAL

5

LEU

ASN

GLU

LEU

LYS

ASP

TYR

ILE

LYS

6

GLN

GLY

CYS

LYS

ARG

SER

ARG

THR

SER

ILE

7

THR

ALA

ARG

THR

LYS

GLU

ALA

GLU

LYS

8

PHE

ALA

ILE

LEU

ILE

LYS

VAL

TYR

ALA

9

GLU

LEU

GLY

TYR

ASN

ASP

ILE

ASN

VAL

THR

10

TRP

ASP

GLY

ASP

THR

VAL

THR

VAL

GLU

GLY

11

GLN

LEU

GLU

GLY

VAL

ASP

Samples:

sample_NC: or34.018, [U-100% 13C; U-100% 15N], 0.369 mM; DTT 5 mM; NaCl 100 mM; Tris-HCl pH 7.5 10 mM; NaN3 0.02%; H2O 90%; D2O 10%

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
3D CCH-TOCSY	sample_NC	isotropic	sample_conditions_1

Software:

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

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

PSVS, Bhattacharya, Montelione - structure validation

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization

NMR spectrometers:

Bruker Avance 800 MHz
Varian INOVA 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks