BMRB Entry 25018

Name: Solution NMR Structure of DE NOVO DESIGNED PROTEIN LFR1 WITH FERREDOXIN FOLD, Northeast Structural Genomics Consortium (NESG) Target OR414
Published: 2014-08-25

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PDB ID: 2mq8
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25018
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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 LFR1 WITH FERREDOXIN FOLD, Northeast Structural Genomics Consortium (NESG) Target OR414

Deposition date:

2014-06-12

Original release date:

2014-08-25

Authors:

Liu, Gaohua; Lin, Yu-Ru; Koga, Nobuyasu; Koga, Rie; Xiao, Rong; Janjua, Haleema; Pederson, Kari; Acton, Thomas; Kornhaber, Gregory; Everett, John; Baker, David; Montelione, Gaetano

Citation:

Citation: Liu, Gaohua; Lin, Yu-Ru; Koga, Nobuyasu; Koga, Rie; Xiao, Rong; Janjua, Haleema; Pederson, Kari; Acton, Thomas; Kornhaber, Gregory; Everett, John; Baker, David; Montelione, Gaetano. "Solution NMR Structure of DE NOVO DESIGNED PROTEIN LFR1 1WITH FERREDOXIN FOLD, Northeast Structural Genomics Consortium (NESG) Target OR414" To be published ., .-..

Assembly members:

Assembly members:
OR414, polymer, 112 residues, 13116.892 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: pET21_NESG

Entity Sequences (FASTA):

Entity Sequences (FASTA):
OR414: MLTVEVEVKITADDENKAEE IVKRVIDEVEREVQKQYPNA TITRTLTRDDGTVELRIKVK ADTEEKAKSIIKLIEERIEE ELRKRDPNATITRTVRTEVG SSWSLEHHHHHH

Data sets:

RDCs
- RDC_list_1
assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	475
15N chemical shifts	107
1H chemical shifts	784
residual dipolar couplings	82

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	OR414	1

Entities:

Entity 1, OR414 112 residues - 13116.892 Da.

1

MET

LEU

THR

VAL

GLU

VAL

GLU

VAL

LYS

ILE

2

THR

ALA

ASP

GLU

ASN

LYS

ALA

GLU

3

ILE

VAL

LYS

ARG

VAL

ILE

ASP

GLU

VAL

GLU

4

ARG

GLU

VAL

GLN

LYS

GLN

TYR

PRO

ASN

ALA

5

THR

ILE

THR

ARG

THR

LEU

THR

ARG

ASP

6

GLY

THR

VAL

GLU

LEU

ARG

ILE

LYS

VAL

LYS

7

ALA

ASP

THR

GLU

LYS

ALA

LYS

SER

ILE

8

ILE

LYS

LEU

ILE

GLU

ARG

ILE

GLU

9

GLU

LEU

ARG

LYS

ARG

ASP

PRO

ASN

ALA

THR

10

ILE

THR

ARG

THR

VAL

ARG

THR

GLU

VAL

GLY

11

SER

TRP

SER

LEU

GLU

HIS

12

HIS

Samples:

sample_NC: OR414, [U-99% 13C; U-98% 15N], 0.885 mM; 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
2D 1H-13C HSQC	sample_NC	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_NC	isotropic	sample_conditions_1

Software:

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinement, structure solution

AutoStructure v2.1, Huang, Tejero, Powers and Montelione - data analysis, refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, data analysis

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

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

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

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

NMR spectrometers:

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