BMRB Entry 25165

Name: Solution NMR Structure of DE NOVO DESIGNED DE NOVO DESIGNED FR55, Northeast Structural Genomics Consortium (NESG) Target OR109
Published: 2014-10-27

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PDB ID: 2mtl
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25165
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Nicholas Rego and David Koes
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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 DE NOVO DESIGNED FR55, Northeast Structural Genomics Consortium (NESG) Target OR109

Deposition date:

2014-08-19

Original release date:

2014-10-27

Authors:

Liu, Gaohua; Koga, Nobuyasu; Koga, Rie; Xiao, Rong; Hamilton, Keith; Ciccosanti, Colleen; Sahdev, Seema; Kohan, Eitan; Acton, Thomas; Kornhaber, Gregory; Everett, John; Baker, David; Montelione, Gaetano

Citation:

Citation: Liu, Gaohua; Koga, Nobuyasu; Koga, Rie; Xiao, Rong; Hamilton, Keith; Ciccosanti, Colleen; Sahdev, Seema; Kohan, Eitan; Acton, Thomas; Kornhaber, Gregory; Everett, John; Baker, David; Montelione, Gaetano. "Solution NMR Structure of DE NOVO DESIGNED DE NOVO DESIGNED FR55, Northeast Structural Genomics Consortium (NESG) Target OR109" To be published ., .-..

Assembly members:

Assembly members:
OR109, polymer, 88 residues, 10233.734 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):
OR109: MGEMDIRFRGDDLEALEKAL KEMIRQARKFAGTVTYTLDG NDLEIRITGVPEQVRKELAK EAERLAKEFNITVTYTIRGS LEHHHHHH

Data sets:

RDCs
- RDC_list_1
- RDC_list_2
assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	377
15N chemical shifts	92
1H chemical shifts	615

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	OR109	1

Entities:

Entity 1, OR109 88 residues - 10233.734 Da.

1

MET

GLY

GLU

MET

ASP

ILE

ARG

PHE

ARG

GLY

2

ASP

LEU

GLU

ALA

LEU

GLU

LYS

ALA

LEU

3

LYS

GLU

MET

ILE

ARG

GLN

ALA

ARG

LYS

PHE

4

ALA

GLY

THR

VAL

THR

TYR

THR

LEU

ASP

GLY

5

ASN

ASP

LEU

GLU

ILE

ARG

ILE

THR

GLY

VAL

6

PRO

GLU

GLN

VAL

ARG

LYS

GLU

LEU

ALA

LYS

7

GLU

ALA

GLU

ARG

LEU

ALA

LYS

GLU

PHE

ASN

8

ILE

THR

VAL

THR

TYR

THR

ILE

ARG

GLY

SER

9

LEU

GLU

HIS

Samples:

sample_NC: OR109, [U-100% 13C; U-100% 15N], 1.01 mM; H2O 90%; D2O 10%

sample_NC5: OR109, [U-5% 13C; U-5% 15N], 1.01 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 4.5; pressure: 1 atm; temperature: 308 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
2D 1H-13C HSQC aliphatic	sample_NC5	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_NC5	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

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

REDCAT, Valafar, Prestegard - geometry optimization

PSVS, Bhattacharya, Montelione - structure validation

NMR spectrometers:

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