BMRB Entry 17304

Name: Solution NMR Structure of de novo designed rossmann 2x3 fold protein, Northeast Structural Genomics Consortium Target OR28
Published: 2010-12-16

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PDB ID: 2l69
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17304
MolProbity Validation Chart

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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 rossmann 2x3 fold protein, Northeast Structural Genomics Consortium Target OR28

Deposition date:

2010-11-17

Original release date:

2010-12-16

Authors:

Liu, Gaohua; Koga, Nobuyasu; Koga, Rie; Xiao, Rong; Mao, Lei; Mao, binchen; Patel, Daya; ciccosanti, colleen; Hamilton, Keith; Acton, Thomas; Baker, David; Montelione, Gaetano

Citation:

Citation: Koga, N.; Koga, R.; Liu, G.; Castellanos, J.; Montelione, G.; Baker, D.. "Role of backbone strain in de novo design of complex alpha/beta protein structures" Nat. Commun. 12, 3921-3921 (2021).
PubMed: 34168113

Assembly members:

Assembly members:
OR28, polymer, 134 residues, 15857.373 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):
OR28: MNIVIVVFSTDEETLRKFKD IIKKNGFKVRTVRSPQELKD SIEELVKKYNATIVVVVVDD KEWAEKAIRFVKSLGAQVLI IIYDQDQNRLEEFSREVRRR GFEVRTVTSPDDFKKSLERL IREVGSLEHHHHHH

Data sets:

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	481
15N chemical shifts	132
1H chemical shifts	975

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	OR28	1

Entities:

Entity 1, OR28 134 residues - 15857.373 Da.

1

MET

ASN

ILE

VAL

ILE

VAL

PHE

SER

THR

2

ASP

GLU

THR

LEU

ARG

LYS

PHE

LYS

ASP

3

ILE

LYS

ASN

GLY

PHE

LYS

VAL

ARG

4

THR

VAL

ARG

SER

PRO

GLN

GLU

LEU

LYS

ASP

5

SER

ILE

GLU

LEU

VAL

LYS

TYR

ASN

6

ALA

THR

ILE

VAL

ASP

7

LYS

GLU

TRP

ALA

GLU

LYS

ALA

ILE

ARG

PHE

8

VAL

LYS

SER

LEU

GLY

ALA

GLN

VAL

LEU

ILE

9

ILE

TYR

ASP

GLN

ASP

GLN

ASN

ARG

LEU

10

GLU

PHE

SER

ARG

GLU

VAL

ARG

11

GLY

PHE

GLU

VAL

ARG

THR

VAL

THR

SER

PRO

12

ASP

PHE

LYS

SER

LEU

GLU

ARG

LEU

13

ILE

ARG

GLU

VAL

GLY

SER

LEU

GLU

HIS

14

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

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

BMRB Entry 17304

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: