BMRB Entry 25612

Name: Solution NMR Structure of DE NOVO DESIGNED Ferredoxin Fold PROTEIN sfr3, Northeast Structural Genomics Consortium (NESG) Target OR358
Published: 2015-09-14

Click here to enlarge.

PDB ID: 2n2u
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25612
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Solution NMR Structure of DE NOVO DESIGNED Ferredoxin Fold PROTEIN sfr3, Northeast Structural Genomics Consortium (NESG) Target OR358

Deposition date:

2015-05-14

Original release date:

2015-09-14

Authors:

Liu, Gaohua; Lin, Yu-Ru; Koga, Nobuyasu; Koga, Rie; Xiao, Rong; Janjua, Haleema; Hamilton, Keith; 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; Hamilton, Keith; Pederson, Kari; Acton, Thomas; Kornhaber, Gregory; Everett, John; Baker, David; Montelione, Gaetano. "Solution NMR Structure of DE NOVO DESIGNED Ferredoxin Fold PROTEIN sfr3, Northeast Structural Genomics Consortium (NESG) Target OR358" To be published ., .-..

Assembly members:

Assembly members:
OR358, polymer, 77 residues, 8898.169 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):
OR358: MVDLKIDVSDDEEAEKIIRE IREQWPKATVTRTNGDIKLD AQTEKEAEKMEKAVKKVKPN ATIRKTGGSLEHHHHHH

Data sets:

RDCs
- RDC_list_1
assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list
- spectral_peak_list_1
- spectral_peak_list_2

Data type	Count
13C chemical shifts	306
15N chemical shifts	70
1H chemical shifts	508
residual dipolar couplings	47

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	OR358	1

Entities:

Entity 1, OR358 77 residues - 8898.169 Da.

1

MET

VAL

ASP

LEU

LYS

ILE

ASP

VAL

SER

ASP

2

ASP

GLU

ALA

GLU

LYS

ILE

ARG

GLU

3

ILE

ARG

GLU

GLN

TRP

PRO

LYS

ALA

THR

VAL

4

THR

ARG

THR

ASN

GLY

ASP

ILE

LYS

LEU

ASP

5

ALA

GLN

THR

GLU

LYS

GLU

ALA

GLU

LYS

MET

6

GLU

LYS

ALA

VAL

LYS

VAL

LYS

PRO

ASN

7

ALA

THR

ILE

ARG

LYS

THR

GLY

SER

LEU

8

GLU

HIS

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_NC	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_NC5	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-15N HSQC	sample_RDC	isotropic	sample_conditions_1

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

BMRB Entry 25612

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: