BMRB Entry 16387

Name: Solution NMR Structure of denovo designed ferrodoxin fold like protein, Northeast Structural Genomics Consortium Target Target OR15
Published: 2009-08-06

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PDB ID: 2kl8
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16387
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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 denovo designed ferrodoxin fold like protein, Northeast Structural Genomics Consortium Target Target OR15

Deposition date:

2009-06-30

Original release date:

2009-08-06

Authors:

Liu, G.; Koga, N.; Jiang, J.; Xiao, R.; Ciccosanti, C.; Locke, J; Everett, J.; Nair, R.; Acton, T; Rost, B; Baker, D; Montelione, G.

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:
OR15, polymer, 85 residues, 10066.570 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: BL21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
OR15: MEMDIRFRGDDLEAFEKALK EMIRQARKFAGTVTYTLDGN DLEIRITGVPEQVRKELAKE AERLAKEFNITVTYTIRLEH HHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	349
15N chemical shifts	84
1H chemical shifts	597

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	OR15	1

Entities:

Entity 1, OR15 85 residues - 10066.570 Da.

1

MET

GLU

MET

ASP

ILE

ARG

PHE

ARG

GLY

ASP

2

ASP

LEU

GLU

ALA

PHE

GLU

LYS

ALA

LEU

LYS

3

GLU

MET

ILE

ARG

GLN

ALA

ARG

LYS

PHE

ALA

4

GLY

THR

VAL

THR

TYR

THR

LEU

ASP

GLY

ASN

5

ASP

LEU

GLU

ILE

ARG

ILE

THR

GLY

VAL

PRO

6

GLU

GLN

VAL

ARG

LYS

GLU

LEU

ALA

LYS

GLU

7

ALA

GLU

ARG

LEU

ALA

LYS

GLU

PHE

ASN

ILE

8

THR

VAL

THR

TYR

THR

ILE

ARG

LEU

GLU

HIS

9

HIS

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D simutaneous 1H, 15N, 13C NOESY	sample_1	isotropic	sample_conditions_1

BMRB Entry 16387

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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